acid-phosphatase and Liver-Diseases

Topics: Acid Phosphatase; Adult; Aged; Alanine Transaminase; Antigen-Antibody Complex; Aspartate Aminotransferases; Enzyme Inhibitors; Female; Humans; Immunoglobulins; Isoenzymes; Liver Diseases; Male; Middle Aged

Topics: Acid Phosphatase; Alkaline Phosphatase; alpha-Amylases; Biliary Tract Diseases; Clinical Enzyme Tests; Enzymes; Female; gamma-Glutamyltransferase; Humans; Isoenzymes; L-Lactate Dehydrogenase; Lipase; Liver Diseases; Metabolism, Inborn Errors; Myocardial Infarction; Nucleotidases; Pancreas; Transaminases; Uterine Neoplasms

Topics: Acid Phosphatase; Adult; Aged; Anesthesia; Biopsy; Esterases; Female; Histocytochemistry; Humans; Liver; Liver Diseases; Liver Glycogen; Middle Aged; Phospholipids; Postoperative Complications; RNA

Microcystins (MC) are hepatotoxic for organisms. Liver MC accumulation and structural change are intensely studied, but the functional hepatic enzymes and energy metabolism have received little attention. This study investigated the liver and hepatocyte structures and the activity of key hepatic functional enzymes with emphasis on energetic metabolism changes after subchronic fish exposure to cyanobacterial crude extract (CE) containing MC. The Neotropical erythrinid fish, Hoplias malabaricus, were exposed intraperitoneally to CE containing 100 μg MC-LR eq kg

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Ammonia; Animals; Aspartate Aminotransferases; Bilirubin; Characiformes; Complex Mixtures; Cyanobacteria; Glucose; Glycogen; Lactates; Lipids; Liver; Liver Diseases; Microcystins; Pyruvates

Microcystins (MC) are frequently present in cyanobacterial blooms in rivers and lakes, increasing the risk of toxicity to both animals and humans. There more than eighty reported microcystins, and the present study was undertaken to determine whether MC-LR and MC-RR can induce different enzyme alterations and histopathological changes in tilapia fish (Oreochromis sp.) exposed to a single intraperitoneal (i.p.) injection of the pure standards (MC-LR and MC-RR) at a dose of 500 mug/kg; the tilapia fish were then observed for seven days. The two MC variants caused significant changes in the activities of acid and alkaline phosphatases (ACP and ALP) in vital organs, showing a different response pattern. The livers and kidneys of fish injected with MC-LR were particularly affected. MC-RR induced a very pronounced increase of ACP in the kidney and a significant increase of ALP in the liver. Both MC variants caused pathological lesions in hepatic tissues, such as megalocytosis, necrotic process, and microvesicular steatosis, particularly in fish treated with MC-LR, and degenerative renal changes, glomerulopathy, were more severe in tilapias exposed to MC-RR. In addition, both microcystins also caused significant myopathy in the heart. In contrast, the gills did not show any change in enzyme activity or histopathological injury.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Bacterial Toxins; Chemical and Drug Induced Liver Injury; Cichlids; Gills; Heart; Injections, Intraperitoneal; Kidney; Kidney Diseases; Liver; Liver Diseases; Microcystins; Myocardium; Organ Size

The present study has been conducted to evaluate the curative effect of propolis extract, a honey bee-hive product, against acetaminophen (APAP) induced oxidative stress and dysfunction in liver and kidney. Animals were challenged with APAP (2 g/kg, p.o.) followed by treatment of propolis extract (100 and 200 mg/kg, p.o.) once only after 24 h. Release of transaminases, alkaline phosphatase, lactate dehydrogenase, and serum bilirubin were increased, whereas hemoglobin and blood sugar were decreased after APAP administration. Antioxidant status in both the liver and kidney tissues were estimated by determining the glutathione, malondialdehyde content and activities of the CYP enzymes, which showed significant alterations after APAP intoxication. In addition, activities of adenosine triphosphatase, acid phosphatase, alkaline phosphatase, and major cell contents (total protein, glycogen and cholesterol) were also altered due to APAP poisoning. Propolis extract successfully reversed the alterations of these biochemical variables at higher dose. Improvements in hepatorenal histoarchitecture were also consistent with biochemical observations. The results indicated that ethanolic extract of propolis has ability to reverse APAP-induced hepatorenal biochemical and histopathological alterations probably by increasing the antioxidative defense activities due to various phenolic compounds present in it.

Topics: Acetaminophen; Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Antioxidants; Bilirubin; Blood Glucose; Chemical and Drug Induced Liver Injury; Cholesterol; Cytochrome P-450 Enzyme System; Dose-Response Relationship, Drug; Female; Glutathione; Glycogen; Hemoglobins; Kidney; Kidney Diseases; L-Lactate Dehydrogenase; Liver; Liver Diseases; Malondialdehyde; Oxidative Stress; Propolis; Rats; Rats, Sprague-Dawley; Silymarin; Transaminases

Lead acetate (300 mg Pb/L) and/or cadmium acetate (10mg Cd/L) in blood and liver were administrated as drinking water to pregnant Wistar rats from day 1 of pregnancy to parturition (day 0) or until weaning (day 21), to investigate the toxic effects in blood and in the liver. Both metals produced mycrocitic anaemia in the pups as well as oxidative damage in the liver, as suggested by the significant increase in TBARS production and the high catalase activity. Moreover, intense alkaline and acid phosphatase activity, used as biomarkers of liver adaptation to damaging factors, was observed. In addition, the toxikinetics are different for Pb and Cd: while Cd is a hepatotoxic from day 0, Pb is not until day 21. Finally, simultaneous perinatal administration of both metals seems to protect, at least, in the liver TBARS production against the toxicity produced by Cd or Pb separately.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Animals, Newborn; Cadmium; Cadmium Poisoning; Catalase; Chemical and Drug Induced Liver Injury; Drug Combinations; Female; Lead; Lead Poisoning; Liver Diseases; Organ Size; Oxidative Stress; Pregnancy; Rats; Rats, Wistar; Thiobarbituric Acid Reactive Substances

Topics: Acid Phosphatase; Alanine Transaminase; Animals; Antibiotics, Antineoplastic; Ascorbic Acid; Aspartate Aminotransferases; Chemical and Drug Induced Liver Injury; Confidence Intervals; Daunorubicin; Liver Diseases; Male; Rats; Rats, Wistar; Vitamin E

We have studied the levels of the biochemical markers of bone formation total serum alkaline phosphatase, osteocalcin (BGP) and carboxyterminal propeptide of type I procollagen (PICP), the levels of the biochemical marker of bone resorption serum tartrate-resistant acid phosphatase (TRAP) and those of intact immunoreactive PTH (iPTH) in 30 patients at different stages of chronic renal failure (CRF), all of them without verifiable hepatopathy, and in 9 patients in hemodialysis with hepatopathy measured by the Knodell index. Sixteen control subjects were also studied. In the group of patients with CRF with or without hepatopathy, the levels of biochemical markers of bone turnover were significantly elevated with respect to those of control patients. We did not find any significant difference in the levels of these parameters between the groups with and without liver damage, in spite of the fact that TRAP and PICP are cleared mainly by the liver. Levels of TRAP and PICP correlated significantly with the other biochemical markers of bone turnover studied. The good relation observed between PICP, TRAP and the biochemical indexes of bone activity and iPTH levels suggests the clinical value of these markers in the follow-up of bone involvement in patients with CRF. On the other hand, the frequent hepatopathy found in patients with CRF does not seem to affect to a significant extent the diagnostic value of PICP and TRAP in this pathology.

Topics: Acid Phosphatase; Adult; Aged; Alkaline Phosphatase; Biomarkers; Bone and Bones; Bone Development; Bone Resorption; Case-Control Studies; Female; Humans; Isoenzymes; Kidney Failure, Chronic; Liver Diseases; Male; Middle Aged; Osteocalcin; Parathyroid Hormone; Peptide Fragments; Procollagen; Renal Dialysis; Tartrate-Resistant Acid Phosphatase

Gaucher disease is the most frequent lysosomal storage disease and the most prevalent genetic disease among the Ashkenazi Jews (q approximately 0.047). The disease results from inherited defects of acid beta-glucosidase and the accumulation of the substrate, glucosylceramide, in cells of monocyte/macrophage origin. The therapeutic response to macrophage-targeted (alpha-mannosyl-terminated) alglucerase (Ceredase, at 60 to 15 IU/kg every 2 weeks) was analyzed in 33 patients (age range, 2 to 63 years; 15 splenectomized) with extensive Gaucher disease over periods of 6 to 24 months. The efficacy of several different doses and dosage reductions was evaluated. In patients with anemia (n = 30) and/or thrombocytopenia (n = 19), hemoglobin levels and platelet counts increased by 0% to 178% and 15% to 155%, respectively, within 3 to 12 months. In patients with splenomegaly (n = 17) and/or hepatomegaly (n = 28), liver and spleen volumes decreased in 6 months from 7% to 64% and 8% to 84% by 12 months, respectively. Hematologic and visceral improvements were noted at any doses between 60 and 15 IU/kg every 2 weeks. Furthermore, these positive initial therapeutic responses were persistent throughout therapy, with doses reduced by 50%. Pulmonary Gaucher disease did not improve clinically in 3 patients. Unrelated cirrhotic (n = 2), cholestatic (n = 1), or renal disease (n = 1) did not influence the rate of patient improvement. Two of five patients who developed serum antibodies against alglucerase during the first 6 to 12 months of therapy had mild antibody reactions. This study shows similar regression of clinical Gaucher disease manifestations with enzyme therapy, using doses between 30 and 60 IU/kg every 2 weeks. Therapeutic efficacy was not diminished after 50% to 75% dose reductions or in the presence of anti-enzyme antibodies.

Topics: Acid Phosphatase; Adolescent; Adult; Anemia; Bone Diseases; Child; Child, Preschool; Gaucher Disease; Glucosylceramidase; Hepatomegaly; Humans; Kidney Diseases; Liver Diseases; Lung Diseases; Middle Aged; Peptidyl-Dipeptidase A; Splenectomy; Splenomegaly; Thrombocytopenia

Lantadene C (22 beta-2-methylbutanoyloxy-3-oxoolean-12-en-28-oic acid) isolated from the leaves of the hepatotoxic plant Lantana camara var. aculeata (Red) has been found to be identical with dihydrolantadene A reported earlier. Molecular structure of lantadene C has been deduced from single crystal X-ray diffraction analysis. It resembles lantadene A in the pentacyclic portion of the molecule but differs in the side chain region. Atom C-34 is cis to C-35 in lantadene C but is trans in lantadene A. Semisynthetic lantadene C was prepared by catalytic hydrogenation of lantadene A. Lantadene C was obtained in two forms, I and II. Form I was crystalline while form II was amorphous. Unlike lantadene A, both form I and II of lantadene C elicited strong hepatotoxic response in guinea pigs associated with decrease in fecal output, feed intake, hepatomegaly, hepatic injury at the cellular and subcellular level, increase in plasma bilirubin, and acid phosphatase activity. All the clinical signs, hepatic lesions, and changes in blood plasma typified lantana toxicity. This is the first report on the hepatoxicity of lantadene C. The interrelation of molecular structure and biological activity of lantadene A and C has been discussed.

Topics: Acid Phosphatase; Animals; Bilirubin; Chemical and Drug Induced Liver Injury; Crystallization; Guinea Pigs; Liver; Liver Diseases; Male; Molecular Structure; Oleanolic Acid; Plant Extracts; Stereoisomerism; Toxins, Biological; X-Ray Diffraction

A combined cytochemical and electron microscopical study has delineated a new type of an erythrocytic inclusion body. Enzyme cytochemically these inclusions are characterized by beta-glucuronidase as a marker enzyme. In part, the inclusions may contain acid phosphatase and ferritin. The inclusions develop in mature erythrocytes since beta-glucuronidase normally does not occur in erythroblasts and, in general, this type of inclusion body is not found in erythroblasts. Based upon our preliminary findings, the hypothesis is extended that beta-glucuronidase is taken up via receptor-mediated endocytosis into erythrocytes and is finally put into clustered cytolysosomal vaculoes, that account for the inclusion bodies as seen at light microscopy. Exogenous beta-glucuronidase might be contributed for by breakdown of cells (e.g. hepatocytes) producing this enzyme in considerable amounts numbers. This view is corroborated by the observation that most patients with beta-glucuronidase-positive inclusions suffered from various chronic disorders of the liver.

Topics: Acid Phosphatase; Adult; Aged; Chronic Disease; Cytoplasm; Erythrocyte Inclusions; Erythrocytes, Abnormal; Female; Ferritins; Glucuronidase; Heinz Bodies; Histocytochemistry; Humans; Liver Diseases; Male; Microscopy, Electron; Middle Aged; Vacuoles

Topics: Acetaminophen; Acid Phosphatase; Animals; Chemical and Drug Induced Liver Injury; Glucose-6-Phosphatase; Liver Diseases; Male; Microsomes, Liver; Phenobarbital; Rats; Rats, Inbred Strains

The maximal activities of liver lysosomal enzymes (acid phosphatase and cathepsin D) were found to be increased in patients with chronic active hepatitis, cirrhosis and primary hepatocellular carcinoma. The ratio between maximal and basal activity (an expression of the degree of retention of the enzymes to lysosome) of acid phosphatase was significantly decreased in patients with chronic active hepatitis and cirrhosis whereas that of cathepsin D did not show any significant changes between normal and various liver disorders. Serum levels of both the enzymes were elevated significantly in patients with cirrhosis and primary hepatocellular carcinoma.

Topics: Acid Phosphatase; Adolescent; Adult; Aged; Cathepsin D; Cathepsins; Chronic Disease; Humans; Liver; Liver Diseases; Lysosomes; Middle Aged; Proteins

A rapid radioassay was used to characterise the adenosine diphosphatase (ADPase) activities in human plasma. There was a major peak at pH 9.3, 80% of whose activity was attributable to non-specific alkaline phosphatase, with the remaining 20% probably due to a specific ADPase. There was also a small peak of ADPase activity at pH 4.0. Inhibitor and chromatographic studies showed that whilst much of this activity was attributable to non-specific acid phosphatase, there was a discrete acid ADPase. Assays of plasma ADPase activities in vascular disorders, including myocardial infarction, peripheral vascular disease and diabetes mellitus, reveal no alterations from control values. Activities of alkaline ADPase were elevated in both chronic and acute liver failure. Acid ADPase was also increased in chronic liver disease and it is suggested that alterations in ADPase activities in liver disorders may contribute to the haemostatic problems observed in these patients.

Topics: Acid Phosphatase; Acute Disease; Alkaline Phosphatase; Apyrase; Chromatography, Gel; Chronic Disease; Humans; Hydrogen-Ion Concentration; Kinetics; Liver Diseases; Myocardial Infarction; Phosphoric Monoester Hydrolases; Vascular Diseases

An enzyme histochemical study was performed to investigate abnormal enzyme activity in human hepatocellular carcinoma (HCC) and, by application of these staining reactions to noncancerous liver disorders, to clarify the true nature of putative percancerous lesions. The enzyme activity of hepatocytes in cirrhotic livers, hepatitis B virus (HBV)-positive cells, and dysplastic liver cells was investigated. Although the tumor cells in HCC gave an intensively positive reaction for gamma-glutamyl transpeptidase activity at the cytoplasm and the whole-cell membrane, they were essentially deficient in glucose-6-phosphatase, alkaline phosphatase, acid phosphatase, and nonspecific esterase activities. Cirrhotic liver showed loss of the orderly zonal difference of enzyme activity that is present in normal liver. However, a pattern of enzyme deviation similar to that of HCC was not recognized anywhere. Neither HBV-positive hepatocytes nor dysplastic liver cells were shown enzymatically to be direct precusors of HCC.

Topics: Acid Phosphatase; Adolescent; Adult; Aged; Alkaline Phosphatase; Carcinoma, Hepatocellular; Cytoplasm; Female; gamma-Glutamyltransferase; Glucose-6-Phosphatase; Hepatitis B Surface Antigens; Humans; Liver; Liver Cirrhosis; Liver Diseases; Liver Neoplasms; Male; Middle Aged; Precancerous Conditions

The activities of the lysosomal enzymes acid and neutral protease, N-acetylglucosaminidase, and acid phosphatase were measured in the serum of patients with fulminant hepatic failure. Acid protease (cathepsin D) activity was increased about tenfold in patients who died and nearly fourfold in those who survived fulminant hepatic failure after paracetamol overdose, whereas activities were increased equally in patients with fulminant hepatic failure due to viral hepatitis whether or not they survived. A correlation was found between serum acid protease activity and prothrombin time, and the increase in cathepsin D activity was sustained over several days compared with aspartate aminotransferase, which showed a sharp early peak and then a fall. Circulating lysosomal proteases can damage other organs, and measurement of their activity may therefore be of added value in assessing prognosis in this condition.

Topics: Acetylglucosaminidase; Acid Phosphatase; Acute Disease; Aspartate Aminotransferases; Humans; Liver Diseases; Lysosomes; Necrosis; Peptide Hydrolases; Prothrombin Time

Qualitative and quantitative analysis was made of morpho-functional and enzymatic changes in the dog liver during long-term extracorporeal circulation. Pronounced necrotic alterations of hepatocytes and microcirculatory disorders were detected by the end of 3-hour extracorporeal circulation. The data obtained indicate the need for correction of circulation in the terminal parts of the vascular bed.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Dogs; Extracorporeal Circulation; Liver; Liver Circulation; Liver Diseases; Male; Microcirculation; Necrosis; Neutral Red; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alanine Transaminase; Animals; Aspartate Aminotransferases; Carbon Tetrachloride Poisoning; Hepatitis, Alcoholic; Humans; Lipid Peroxides; Liver Diseases; Lysosomes; Male; Rats

The authors have measured the activity of acid phosphatase, beta-glucuronaidase and cathepsin-D in tthe sera of patients with different liver diseases, and the actvity of beta-glucuronidase in granulocytes and the rate of its release. Using the method for the releaseof beta-glucuronidase from the granulocytes they drew conclusions to thedegree of the membrane-damage occurring in the liver diseases. They provided that in the sera of patients with different liver diseases the increase in the activity of the acid phosphatase and the beta-glucuronidase is different. According to their in vitro studies the decrease in the beta-glucuronidase activity measured in the granulocytes, and the release of enzyme is in connection with the type of liver disease and with the different degree of lysosomal membrane alteration.

Topics: Acid Phosphatase; Adolescent; Adult; Aged; Chronic Disease; Female; Glucuronidase; Granulocytes; Hepatitis; Humans; Liver Cirrhosis; Liver Diseases; Lysosomes; Male; Middle Aged

Lysosome are subcellular particles in which several acid hydrolases of various specificities are localized. The role of lysosome in cellular physiology and pathology has drawn considerable recent attention by several groups of investigators. The purpose of this study was to investigate the activities of lysosomal enzymes--acid phosphatase, beta-glucuronidase, N-acetyl-beta-glucosaminidase--in hepatic disorders. 1) The serum levels of beta-glucuronidase and N-acetyl-beta-glucosaminidase were significantly elevated in patients with diseases of the hepatobiliary system. 2) N-acetyl-beta-glucosaminidase activity in urine specimens from patients with diseases of the hepatobiliary system was found to be significantly higher than in urine specimens from normal adults. 3) Male albino rats of 150 approximately 200 g body weight were used. CCl4 was injected intraperitoneally (dose 0.1 ml of CCl4 per 100 g body weight twice a week for eight weeks). The free activities of lysosomal enzyme were increased and high free/total activity ratios were found in the liver lysosomal fraction of CCl4 intoxicated rats. The results of these experiment indicated that the membranes of lysosome were more permeable to their enzymes, and the release of these enzymes were found in the experimental fatty liver by CCl4. 4) Corticosteroids and chloroquine stabilized rat liver lysosome in vitro from the labilizing influence of incubation at 37 degrees C. 5) The administration of chloroquine to CCl4 intoxicated rats did not cause any well-expressed stabilization of lysosomes. 6) When alpha-Tocopherol was administrated to CCl4 intoxicated rats, the decrease of bound activity and increase of free activity in lysosomal fraction, and increase of acid hydrolases, GOT and GPT in serum were inhibited.

Topics: Acid Phosphatase; Animals; Chemical and Drug Induced Liver Injury; Chloroquine; Glucuronidase; Hexosaminidases; Humans; Jaundice; Liver Diseases; Liver Neoplasms; Lysosomes; Male; Rats; Vitamin E

Of 146 patients with lymphogranulomatosis biochemical parameters were tested for their diagnostic valency concerning the recognition of a liver infiltration. In patients with histologically proved affection of the liver the AP, GGTP, AAP, LAP and LDH show a significant increase in comparison to the enzyme values of the patients without any hepatic manifestation. In an increased result of 4 enzyme values with a probability of 85% muste be reckoned with a participation of the liver. The enzyme SGOT, SGPT, GDH, LDH-isoenzymes, choline esterase, beta-GC, the De Ritis quotient and the quotient (Formula: see text), on the other hand, do not give any additional differential-diagnostic information.

Topics: Acid Phosphatase; Alanine Transaminase; Aspartate Aminotransferases; Cholinesterases; Female; Glucuronidase; Glutamate Dehydrogenase; Hodgkin Disease; Humans; Isoenzymes; L-Lactate Dehydrogenase; Liver; Liver Diseases; Male

The effects of acute and chronic administration of D-Galactosamine (GalN), Ethanol and Phenobarbital were investigated on the activities of lysosomal enzymes, i.e.; acid phosphatase, beta-glucuronidase and n-acetyl-beta-glucosaminidase, and others such as gamma-GTP and adenosine triphosphatase. The histochemical distribution of gamma-GTP in the liver was also studied on biopsy specimens from patients with chronic hepatitis, and gamma-GTP levels in the serum of patients receiving drugs inductable of hepatic microsomal enzymes. 1) After a single intraperitoneal injection of GalN, the lysosomal enzyme activities were lowered in the necrotic areas, but raised in the perinecrotic areas, the proliferative Kupffer cells and intra- and/or extra-cellular eosine bodies. 2) gamma-GTP activities in rat liver after chronic administration of GalN were markedly increased in bile canalicular membrane of periportal parenchymal cells, the epithelium of bile duct and ductules, and som inflammatory cells of portal fields. Levels of serum gamma-GTP were also elevated. On histochemical studies with biopsy specimens from patients with chronic active hepatitis showing elevated gamma-GTP activity, the activity was revealed a similar localization to GalN-treated rats. These data suggested that the increased activities might be reflected on the active stage in chronic hepatitis. 3) Chronic ethanol treatment in rats induced clearly-stained lysosomes varied in size, especially large-sized. The activities of hepatic gamma-GTP were slightly increased in the bile canalicular membrane of periportal parenchymal cells and the epithelium of proliferative bile ductules. 4) It has been shown by histochemical and biochemical techniques that hepatic gamma-GTP activity was increased after phenobarbital administration in rats. A significant rise in serum gamma-GTP was observed in patients on long-term treatment with anti-epileptic drugs. These data indicated that the increased activities of serum gamma-GTP might be accompanied with induction of hepatic microsomal drug-metabolizing enzymes.

Topics: Acetylglucosaminidase; Acid Phosphatase; Adenosine Triphosphatases; Alcoholism; Animals; Anticonvulsants; Chemical and Drug Induced Liver Injury; Ethanol; Galactosamine; gamma-Glutamyltransferase; Glucuronidase; Histocytochemistry; Humans; Liver; Liver Diseases; Lysosomes; Male; Phenobarbital; Rats

Stokke has described a lysosomal cholesterol ester hydrolase (CEH) in human liver. To clarify the significance of this enzyme, we first modified Stokke's assay to enable CEH determination in hepatic needle biopsies. Studies established optimal pH of 4.6--5.2 and linearity of hydrolysis for at least 12 hours, using homogenates containing about 2 mg liver and radiolabeled cholesterol oleate as substrate. The assay was then applied to patients undergoing percutaneous needle biopsy. Hepatic CEH activity in alcoholic liver disease, obstructive jaundice and a variety of other hepatic disorders was not significantly different from that in histologically normal livers. In patients with acute hepatitis, however, mean CEH activity was more than 3-fold increased (P less than 0.01). Values paralleled SGOT levels, returned to normal as hepatitis resolved, and were unrelated to serum cholesterol levels or to lecithin:cholesterol acyltransferase activity. In contrast to CEH, activity of acid phosphatase, a standard lysosomal marker enzyme, was the same in hepatitic as in normal livers. We conclude that CEH can be assayed in needle biopsies of human liver, that its activity increases in acute hepatitis, and that this is probably not simply due to a nonspecific general increase in lysosmal enzymes.

Topics: Acid Phosphatase; Cholesterol Esters; Humans; Hydrolases; Liver; Liver Diseases; Liver Function Tests; Phosphatidylcholine-Sterol O-Acyltransferase

Topics: Acid Phosphatase; Animals; Chemical and Drug Induced Liver Injury; Endotoxins; Injections, Intraperitoneal; Liver; Liver Diseases; Male; Necrosis; Rats

In normal mongrel dogs, outflow occlusion of 15 or 30 minutes duration was produced by clamping both the suprahepatic and suprarenal portions of the vena cava. One dog died immediately after release of occlusion; two dogs died from recurrent hypotension between six and 24 hours postoperatively. The other five dogs survived for three days, at which time an autopsy was done. During outflow occlusion, the blood pressure fell in all dogs, as did the central venous pressure. The pulse rate decreased during, and after, occlusion but toward a tendency of gradual recovery. A significant drop in pH and base excess of arterial blood was seen after occlusion. Although a steady, but not substantial, increase in hemoglobin and hematocrit values was noted, there were no remarkable changes in the blood coagulation system. Significant increases in serum glutamic-oxalacetic transaminase, glutamic-pyruvic-transaminase, lactic dehydrogenase, acid phosphatase and beta-glucuronidase activities were observed from immediately after release of occlusion, but alkaline phosphatase values increased much later than did these. Thus, hepatic outflow occlusion, even if it is short, seems to be dangerous in the dog, since it produces hypotension, metabolic acidosis and diffuse damage as well as disruption of the parenchyma of the liver.

Topics: Acid Phosphatase; Acid-Base Equilibrium; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Blood; Blood Pressure; Central Venous Pressure; Dogs; Female; Glucuronidase; Hemodynamics; Hydrogen-Ion Concentration; L-Lactate Dehydrogenase; Liver Circulation; Liver Diseases; Male

An increased stability of liver lysosomes and mitochondria of burned, dehydrated and tumour-bearing rats has been found in the present investigations. Using biochemical criteria we were able to show that the membranes of liver subcellular particles of these animals become more resistent to the labilizing action of CCl4. The latter effect was confirmed by electron microscopic data. The tumour growth, dehydration and burning of rats as well as sleep deprivation, overheating, lanthanum and ruthenium red have been shown to cause changes in the activity of some enzyme-systems located in endoplasmic reticulum. The protective action of these chemical, pathological and stress factors against CCl4 produced damage to the cell organelles studied is discussed in relation to the activity of the drug metabolizing pathways; biochemical (modifying of some enzyme activity) as well as pharmacological (duration of hexobarbital sleep) data were used as criteria for the activity of these pathways.

Topics: Acid Phosphatase; Aniline Hydroxylase; Animals; Burns; Carbon Tetrachloride; Chemical and Drug Induced Liver Injury; Dehydration; Endoplasmic Reticulum; Female; Liver; Liver Diseases; Lysosomes; Male; Microscopy, Electron; Mitochondria, Liver; Oxygen Consumption; Rats; Stress, Physiological

Topics: Acid Phosphatase; Biliary Tract Diseases; Clinical Enzyme Tests; Histidine Ammonia-Lyase; Humans; L-Lactate Dehydrogenase; Liver Diseases; Urokinase-Type Plasminogen Activator

A histochemical study of plasma-membrane associated enzymes in rat liver demonstrated a significant lesion 3 days after a single oral dose of 2,3,7,8-tetrachlorodibenzo-p-dioxin (dioxin). The complete loss of canalicular ATPase reaction in the parenchymal cells of the centrilobular zone remained the prominent feature of the liver throughout the 6-wk period studied. Involvement of the periportal and midzonal regions occurred in moribund animals and improvement in the health of two surviving animals at 9 mth was associated with a normal distribution of ATPase in the liver. Qualitative changes in 5-nucleotidase and acid phosphatase were secondary to the parenchymal cell damage. This lesion supports the morphological evidence, reported previously, that the parenchymal cell plasma-membrane is a specific subcellular site of the toxic action of dioxin.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Cell Membrane; Chemical and Drug Induced Liver Injury; Dioxins; Female; Histocytochemistry; Liver; Liver Diseases; Nucleotidases; Polychlorinated Dibenzodioxins; Rats; Time Factors

In the course of liver injury induced by CCl4 in rats the change of the endoplasmic reticulum takes 5 hours and that of the lysosomal membrane, 18 hours to develop. The latter change precedes hepatocellular necrosis. Elevation of plasma free fatty acids and fatty infiltration of the liver can be observed at 3 hours after CCl4 administration. The maximum of fatty infiltration, hepatocellular necrosis and the highest degree of lysosomal damage develop at the same time. Since CCl4 is eliminated in a few hours, it must initiate a cellular process which then leads to lysosomal membrane damage and hepatocellular necrosis.

Topics: Acid Phosphatase; Animals; Carbon Tetrachloride; Carbon Tetrachloride Poisoning; Chemical and Drug Induced Liver Injury; Cytosol; Fatty Acids, Nonesterified; Female; Glucose-6-Phosphatase; Lipid Metabolism; Liver; Liver Diseases; Lysosomes; Male; Necrosis; Rats; Time Factors

Rats were killed at various time-intervals up to 48 hr after a single large dose of paracetamol (3 g per kg) and their livers examined by light and electron microscopy. In general, this revealed glycogen depletion, loss of ribosomes, and cytoplasmic matrix swelling commencing 3-6 hr after administration which in centrilobular hepatocytes progressed to frank coagulative necrosis at 12-24 hr. Midzonal cells showed more prominent aqueous swelling with besiculation of the endoplasmic reticulum, and in some cells, gross hydropic vacuolation.

Topics: Acetaminophen; Acid Phosphatase; Animals; Chemical and Drug Induced Liver Injury; Endoplasmic Reticulum; Histocytochemistry; Liver; Liver Diseases; Lysosomes; Macrophages; Male; Microscopy, Electron; Necrosis; Rats; Rats, Inbred Strains; Ribosomes; Succinate Dehydrogenase; Time Factors; Vacuoles

Topics: Acid Phosphatase; Alkaline Phosphatase; Esterases; Humans; Kupffer Cells; Lipase; Liver Diseases

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Cell Nucleus; DNA; Glucose-6-Phosphatase; Glucuronidase; L-Lactate Dehydrogenase; Liver; Liver Diseases; Mice; Mitosis; Nucleotidases; Plant Poisoning; Succinate Dehydrogenase; Toxins, Biological; Triglycerides

Topics: Acid Phosphatase; Acute Disease; Adult; Alkaline Phosphatase; Autopsy; Electron Transport Complex IV; Female; Glucosephosphate Dehydrogenase; Glycerolphosphate Dehydrogenase; Histocytochemistry; Humans; Hydroxybutyrate Dehydrogenase; L-Lactate Dehydrogenase; Liver; Liver Diseases; NAD; Peroxidases; Porphyrias; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Carbon Disulfide; Cell Membrane; Chemical and Drug Induced Liver Injury; Edema; Endoplasmic Reticulum; Glucose-6-Phosphatase; Histocytochemistry; Liver; Liver Diseases; Male; Mixed Function Oxygenases; Nucleotidases; Phenobarbital; Rats; Starvation; Succinate Dehydrogenase; Time Factors

Topics: Acid Phosphatase; Animals; Chemical and Drug Induced Liver Injury; Esterases; Female; Glycogen; Histocytochemistry; L-Lactate Dehydrogenase; Lanthanum; Liver; Liver Diseases; Malate Dehydrogenase; Male; Phosphorylase Kinase; Rats; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alkaloids; Ammonium Sulfate; Animals; Chemical and Drug Induced Liver Injury; Dithiothreitol; DNA-Directed RNA Polymerases; Glucuronidase; Hemolysis; Liver; Liver Diseases; Organ Size; Peptides; Perfusion; Potassium; Rats; Temperature

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Carbon Disulfide; Chemical and Drug Induced Liver Injury; Histocytochemistry; Liver; Liver Diseases; Potassium; Rats; Sodium; Water

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adult; Aged; Biopsy; Female; Glucuronidase; Hepatitis; Histocytochemistry; Humans; Liver; Liver Diseases; Male; Middle Aged

Topics: Acid Phosphatase; Alkaline Phosphatase; Amniocentesis; Amniotic Fluid; Antibody Formation; Bilirubin; Birth Weight; Blood; Estrogens; Female; Hemoglobins; Humans; Liver Diseases; Pregnancy; Pregnancy Complications; Progesterone; Proteins; Rh-Hr Blood-Group System; Time Factors; Umbilical Cord

Topics: Acid Phosphatase; Administration, Oral; Animal Feed; Animals; Blood Proteins; Bursa of Fabricius; Capillary Fragility; Chemical and Drug Induced Liver Injury; Chickens; Fusarium; Hematoma; Hemoglobins; Lipids; Liver; Liver Diseases; Mycotoxins; Organ Size; Pancreas; Poultry Diseases; Spleen

Topics: Acid Phosphatase; Alkaline Phosphatase; Amylases; Biliary Tract Diseases; Bone Diseases; Clinical Enzyme Tests; Creatine Kinase; Enzymes; Humans; Isoenzymes; Liver Diseases; Male; Muscular Diseases; Myocardial Infarction; Nervous System Diseases; Organ Specificity; Oxidoreductases; Pancreatic Diseases; Prostatic Diseases; Pulmonary Embolism; Transaminases

Topics: Acid Phosphatase; Acute Disease; Adenosine Triphosphatases; Adult; Aged; Alcoholism; Alkaline Phosphatase; Biopsy; Chemical and Drug Induced Liver Injury; Cholestasis; Chronic Disease; Enzymes; Fatty Liver; Female; Hepatitis A; Histocytochemistry; Humans; Hydroxybutyrate Dehydrogenase; Liver; Liver Cirrhosis; Liver Diseases; Male; Middle Aged

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Chemical and Drug Induced Liver Injury; Choline; Galactosamine; Hepatitis A; Histocytochemistry; Humans; Liver Diseases; Orotic Acid; Rats; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Cardiolipins; Cell Fractionation; Centrifugation, Density Gradient; Chromatography, Thin Layer; Hydrogen-Ion Concentration; Lipid Metabolism, Inborn Errors; Liver; Liver Diseases; Lysosomes; Male; Mitochondria, Liver; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylinositols; Phospholipids; Rats; Sphingomyelins; Surface-Active Agents

The distribution of Brucella melitensis in various tissues and in subcellular fractions obtained from liver was investigated to evaluate the initial phases of brucellosis in the guinea pig. Fifty minutes after intravenous infection, brucellae were found principally in the blood and liver, with a substantial number recovered from spleen. Fractionation of liver established that most bacteria were found in the mitochondrial plus lysosomal (M + L) fraction; a significant number, however, sedimented in the nuclear (N) fraction. With time, there was a progressive shift of bacteria from the M + L to the N fraction, accompanied by a similar shift in acid phosphatase activities. Isopycnic centrifugation of mixtures of M + L fractions and brucellae permitted complete separation of acid phosphatase-bearing particles from bacteria. Similar experiments with fractions from infected animals showed that viable bacteria were found in both the acid phosphatase and free brucellae regions of the gradient. At 10 min postinfection, 52% of the recovered organisms were in the acid phosphatase region; at 30 min, 65%; at 60 min, 85%; and at 315 min, 79%. Detergent plus sonic treatment of an M + L fraction from the liver of an animal killed 50 min after infection caused most of the bacteria in the acid phosphatase region to shift to the region where free bacteria were found. These data suggested that brucellae sequestered in the liver were located primarily in the vacuolar apparatus of the cells which phagocytized them.

Topics: Acid Phosphatase; Animals; Brucella; Brucellosis; Centrifugation, Density Gradient; Culture Media; Cytoplasm; Guinea Pigs; Inclusion Bodies; Injections, Intravenous; Kidney; Liver; Liver Diseases; Lung; Lysosomes; Myocardium; Phagocytosis; Phosphorus Isotopes; Sepsis; Spleen; Subcellular Fractions

Topics: Acid Phosphatase; Alkaline Phosphatase; Biopsy; Diabetes Mellitus; Fatty Liver; Glutamate Dehydrogenase; Histocytochemistry; Humans; L-Lactate Dehydrogenase; Liver; Liver Diseases; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alkaline Phosphatase; Blood Proteins; Child, Preschool; Egypt; Female; Fructose-Bisphosphate Aldolase; Humans; Infant; Infant, Newborn; Kwashiorkor; L-Lactate Dehydrogenase; Liver; Liver Diseases; Male; Proteins

Topics: Acid Phosphatase; Bone Diseases; Bone Marrow; Humans; Hyperparathyroidism; Kidney; Kidney Diseases; Liver; Liver Diseases; Male; Neoplasms; Parathyroid Glands; Prostate; Prostatic Neoplasms; Spleen

Topics: Acid Phosphatase; Humans; Liver; Liver Diseases

Topics: Acid Phosphatase; Animals; Atrophy; Cytoplasmic Granules; Endoplasmic Reticulum; Histiocytes; Histocytochemistry; Ligation; Liver; Liver Circulation; Liver Diseases; Lysosomes; Male; Microscopy, Electron; Mitochondria, Liver; Necrosis; Organoids; Portal Vein; Rats; Staining and Labeling

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Bile Pigments; Biopsy; Central Nervous System; Chemical and Drug Induced Liver Injury; Copper; Esterases; Fatty Liver; Female; Glutamate Dehydrogenase; Hemolysis; Histocytochemistry; Liver; Liver Diseases; Necrosis; Organ Size; Sheep; Sheep Diseases; Succinate Dehydrogenase; Sulfates

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Carcinogens; Carcinoma, Hepatocellular; Fluorenes; Glucose-6-Phosphatase; Glucuronidase; Glycogen; Histocytochemistry; Hyperplasia; L-Lactate Dehydrogenase; Liver Diseases; Liver Neoplasms; Male; Neoplasms, Experimental; Phosphorylase Kinase; Rats; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Bile Ducts; Biliary Tract Diseases; Bone and Bones; Carcinoma, Hepatocellular; Chemical and Drug Induced Liver Injury; Chromatography, Gel; Chromatography, Ion Exchange; Electrophoresis; Intestines; Isoenzymes; Kidney; Ligation; Liver; Liver Diseases; Liver Neoplasms; Male; Neoplasms, Experimental; Rats

Topics: Acid Phosphatase; Biliary Tract Diseases; Blood Platelets; Bone and Bones; Breast Neoplasms; Erythrocytes; False Positive Reactions; Female; Formaldehyde; Humans; Hydrogen-Ion Concentration; Kidney; Kidney Diseases; Liver; Liver Diseases; Male; Neoplasms; Phenolphthaleins; Phosphates; Prostate; Prostatic Diseases; Prostatic Neoplasms; Tartrates

Topics: Acid Phosphatase; Adult; Aged; Alanine Transaminase; Alkaline Phosphatase; Aspartate Aminotransferases; Cholangitis; Granuloma; Humans; L-Lactate Dehydrogenase; Liver; Liver Diseases; Male; Middle Aged

Topics: Acid Phosphatase; Animals; Atrophy; Cytoplasm; Disease Models, Animal; Histocytochemistry; Liver; Liver Diseases; Liver Glycogen; Male; Microscopy, Electron; Phagocytosis; Rats

Topics: Acid Phosphatase; Adolescent; Child; Child, Preschool; Glycosaminoglycans; Humans; Lipidoses; Liver; Liver Diseases; Lysosomes; Male; Microscopy, Electron

Topics: Acid Phosphatase; Adolescent; Child; Child, Preschool; Chronic Disease; Esterases; Fatty Liver; Glycerolphosphate Dehydrogenase; Hepatitis; Histocytochemistry; Humans; Hypertension, Portal; Liver; Liver Cirrhosis; Liver Diseases; Malate Dehydrogenase; Succinate Dehydrogenase

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Alkaloids; Animals; Chemical and Drug Induced Liver Injury; Electron Transport Complex IV; Esterases; Glucose-6-Phosphatase; Glutamate Dehydrogenase; Heterocyclic Compounds; Histocytochemistry; Kidney Diseases; Kidney Tubules; Liver; Liver Diseases; Male; Necrosis; Rats; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Atrophy; Ischemia; Liver Circulation; Liver Diseases; Liver Glycogen; Portal Vein; Rats

The peroxidatic activity of hemoglobin permitted visualization of its uptake by rat hepatocytes by means of the Graham-Karnovsky 3,3'-diaminobenzidine (DAB) procedure. Lysosomes were visualized by their acid phosphatase, beta-glucuronidase, and glucosaminidase activities. When large doses of rat, cow, or human hemoglobin are intravenously injected, or when hemoglobinemia is induced by injection of distilled water, DAB-positive hemoglobin is engulfed by pinocytosis. Pinocytotic vacuoles become digestive vacuoles ("phagolysosomes") by fusion with lysosomes of the dense body type that have moved from their pericanalicular position. By 16-24 hr after even massive amounts of hemoglobin (400 mg/100 g), the protein is barely demonstrable in hepatocytes. At the lowest doses of injected hemoglobin (15 mg/100 g body weight), DAB-positive vacuoles are demonstrable only in the Kupffer cells.

Topics: Acid Phosphatase; Animals; Cattle; Glucosyltransferases; Glucuronidase; Hemoglobins; Hemosiderosis; Humans; Injections, Intravenous; Liver; Liver Diseases; Lysosomes; Microscopy, Electron; Peroxidases; Pinocytosis; Rats; Time Factors

Topics: Acid Phosphatase; Animals; Hemorrhage; Liver; Liver Diseases; Necrosis; Rats; Transducers; Ultrasonics

Topics: Acid Phosphatase; Adolescent; Adult; Biopsy; Blind Loop Syndrome; Female; Gastrectomy; Gastric Juice; Glucose-6-Phosphatase; Histocytochemistry; Humans; Hyperthyroidism; Intestinal Mucosa; Intestine, Small; Iodine Isotopes; Lipase; Liver Diseases; Male; Sjogren's Syndrome; Succinate Dehydrogenase; Triolein

Topics: Acid Phosphatase; Animals; Cytoplasmic Granules; Histocytochemistry; Liver Diseases; Methods; Mice; Schistosomiasis; Time Factors

Topics: Acid Phosphatase; Alkaline Phosphatase; Clinical Enzyme Tests; Creatine Kinase; Enzymes; Female; Humans; Isoenzymes; Liver Diseases; Male; Metabolism, Inborn Errors; Muscular Diseases; Myocardial Infarction; Transaminases

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adult; Alkaline Phosphatase; Angina Pectoris; Animals; Aortic Diseases; Blood Proteins; Chromatography; Chromatography, Gel; Diabetes Mellitus; Dogs; Electrocardiography; Electrophoresis; Female; Heart Failure; Humans; Hypertension; Isoenzymes; Kidney; Kidney Diseases; Liver; Liver Diseases; Lysosomes; Male; Mesenteric Arteries; Middle Aged; Mitochondria; Muscles; Myocardium; Potassium; Radionuclide Imaging; Rats; Sodium; Transaminases

Topics: Acid Phosphatase; Animals; Cathepsins; Deoxyribonucleases; Ischemia; Liver Diseases; Lysosomes; Male; Rats; Ribonucleases; Solubility; Sulfatases

Topics: Acid Phosphatase; Acute Disease; Age Factors; Alkaline Phosphatase; Animals; Avitaminosis; Bone Neoplasms; Carcinoma; Chronic Disease; Diabetes Mellitus; Esophageal Neoplasms; Estrus; Female; Hematologic Diseases; Hemoglobinuria, Paroxysmal; Histocytochemistry; Hodgkin Disease; Humans; Infections; Leukemia; Leukocytes; Liver Diseases; Lung Neoplasms; Male; Myocardial Infarction; Neutrophils; Pregnancy; Prostatic Neoplasms; Radiation Injuries; Stress, Physiological

Topics: Acid Phosphatase; Animals; Diet; Female; Galactosidases; Glucuronidase; Hydrolases; Liver Diseases; Lysosomes; Male; Necrosis; Rats; Testicular Diseases; Testis; Vitamin E Deficiency

Topics: Acid Phosphatase; Alkaloids; Animals; Chemical and Drug Induced Liver Injury; Esterases; Histocytochemistry; Liver Diseases; Lysosomes; Male; Rats

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Deoxyribonucleases; Histocytochemistry; Humans; Liver; Liver Diseases; Morphine; Morphine Dependence; Rats; RNA

Topics: Acid Phosphatase; Alcohol Oxidoreductases; Alkaline Phosphatase; Animals; Carbon Tetrachloride Poisoning; Carbonic Anhydrases; Dihydrolipoamide Dehydrogenase; Electron Transport Complex IV; Esterases; Histocytochemistry; L-Lactate Dehydrogenase; Liver; Liver Diseases; Male; Mice; Succinate Dehydrogenase; Zinc

Topics: Acid Phosphatase; Hepatitis A; Histocytochemistry; Humans; Hyperbilirubinemia; Jaundice; Liver; Liver Cirrhosis; Liver Diseases

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Female; Histocytochemistry; Humans; Liver; Liver Diseases; Pregnancy; Pregnancy Complications

Topics: Acid Phosphatase; Adenosine Triphosphatases; Adenosine Triphosphate; Adult; Aged; Alkaline Phosphatase; Bilirubin; Female; Heart Failure; Humans; Hydrogen-Ion Concentration; Hypertension; Liver Diseases; Male; Middle Aged; Phenolphthaleins; Phosphoric Monoester Hydrolases; Temperature; Transaminases

Topics: Acid Phosphatase; Bile Duct Neoplasms; Geriatrics; Jaundice; Jaundice, Obstructive; Liver Diseases; Pancreatic Neoplasms

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Glucose-6-Phosphatase; Glutamate Dehydrogenase; Histocytochemistry; In Vitro Techniques; Liver; Liver Diseases; Mice; Necrosis; Nucleotidases; Rats; Research; Succinate Dehydrogenase; Tissue Culture Techniques

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Arginase; Aspartate Aminotransferases; Catalase; Clinical Enzyme Tests; Enzymes; Fructose-Bisphosphate Aldolase; Glucose-6-Phosphatase; Humans; In Vitro Techniques; Liver; Liver Diseases; Liver Function Tests; Liver Neoplasms

Topics: Acid Phosphatase; Alkaline Phosphatase; Communicable Diseases; Diabetes Mellitus; Gastrointestinal Diseases; Gastrointestinal Neoplasms; Heart Diseases; Hematologic Diseases; Humans; Kidney Diseases; Leukocytes; Liver Diseases; Lung Neoplasms; Mental Disorders; Neurologic Manifestations; Thyroid Diseases

Topics: Acid Phosphatase; Animals; Cytoplasm; Cytoplasmic Granules; Hypoxia; Liver; Liver Diseases; Lysosomes; Microscopy, Electron; Rats

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Aspartate Aminotransferases; Carbohydrate Metabolism; Cholinesterases; Clinical Enzyme Tests; D-Alanine Transaminase; Edema; Fructose-Bisphosphate Aldolase; Glucose-6-Phosphatase; Heart Failure; Humans; Isomerases; L-Lactate Dehydrogenase; Liver Circulation; Liver Diseases; Liver Function Tests; Pericarditis; Pleural Effusion; Proteins; Rabbits

Topics: Acid Phosphatase; Alkaline Phosphatase; Anaphylaxis; Animals; Dermatitis; Electron Transport Complex II; Histocytochemistry; Liver; Liver Diseases; Liver Glycogen; Metabolism; Rabbits; Research; Shwartzman Phenomenon; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Croton Oil; Dermatitis; Electron Transport Complex II; Histocytochemistry; Liver; Liver Diseases; Liver Glycogen; Metabolism; Rabbits; Research; Succinate Dehydrogenase

Topics: Acid Phosphatase; Cytoplasm; Glucuronidase; Hydrogen-Ion Concentration; Hydrolases; Liver; Liver Diseases; Liver Regeneration; Mitochondria; Osmosis; Osmotic Pressure; Solutions; Sucrose

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Amylases; Aspartate Aminotransferases; Clinical Enzyme Tests; Creatine Kinase; D-Alanine Transaminase; Diagnosis, Differential; Humans; Liver Diseases; Muscular Diseases; Myocardial Infarction; Pancreatitis

Topics: Acid Phosphatase; Biliary Tract; Child; Chronic Disease; Clinical Enzyme Tests; Duodenum; Endopeptidases; Enteropeptidase; Gastrointestinal Diseases; Humans; Liver Diseases

Topics: Acid Phosphatase; Ceroid; Liver; Liver Diseases; Mice; Necrosis; Nutrition Disorders; Pigments, Biological; Rats; Research

Topics: Acid Phosphatase; Administration, Intravenous; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Blood Chemical Analysis; D-Alanine Transaminase; Electron Transport Complex II; Heart Diseases; Liver Diseases; Necrosis; Papain; Pathology; Rabbits; Research; Succinate Dehydrogenase

Topics: Acid Phosphatase; Alkaline Phosphatase; Bile; Cell Nucleus; Cholestasis; Cytomegalovirus Infections; Giant Cells; Hepatitis; Humans; Infant; Infant, Newborn; Jaundice; Liver; Liver Diseases; Liver Regeneration; Pathology

Topics: 5'-Nucleotidase; Acid Phosphatase; Alkaline Phosphatase; Biliary Tract; Biliary Tract Diseases; Bone Diseases; Disease; DNA; Leucyl Aminopeptidase; Liver Diseases; Pancreas; Pancreatic Diseases; Peptide Hydrolases; Phosphoric Monoester Hydrolases; Protein Tyrosine Phosphatases; RNA; Trees

Topics: Acid Phosphatase; Blood; Digestion; Humans; Liver Diseases; Male; Phosphoric Monoester Hydrolases; Prostatic Neoplasms

Topics: Acid Phosphatase; Hepatic Insufficiency; Liver Diseases; Phosphoric Monoester Hydrolases