acid-phosphatase and Edema

The anti-cancer drug cyclophosphamide (CYP) is nephrotoxic besides being urotoxic thereby limiting its clinical utility. Since the nephrotoxicity of CYP is less common compared to its urotoxicity, not much importance has been given for the study of mechanism of CYP-induced nephrotoxicity. The aim of the present study is to investigate the possible role of lysosomal enzymes in CYP-induced renal damage. Adult female Wistar rats weighing 200-250 g were used for the study. The rats were administered single-intraperitoneal injection of CYP at the dose of 150 mg/kg body wt and sacrificed at various time intervals 6, 16 or 24 h after the dose of CYP. The control rats were administered saline alone. Nephrotoxicity was assessed by measuring plasma creatinine and urea and histopathology of the kidney. The kidney was weighed and used for the assay of lysosomal enzymes namely acid phosphatase, beta-glucuronidase and N-acetylglucosaminidase and total protein content. Histologically, the CYP-treated rat kidneys showed progressive renal damage with increase in time after treatment. Glomerular nephritis, cortical tubular vacuolization and interstitial edema were observed in the CYP-treated rats. Surprisingly, a significant drastic decrease (instead of an increase) in the activities of lysosomal enzymes was observed in the kidneys of CYP-treated rats at 16 and 24 h as compared with the control. A highly significant increase (270%) in protein content was observed in the kidneys of the CYP-treated rats as compared with the control. Decrease in the activities of lysosomal protein digestive enzymes may contribute to CYP-induced renal damage. The accumulation of abnormal amounts of the protein in the kidney may be due at least in part to defect in lysosomal enzyme activity and contribute to renal damage.

Topics: Acetylglucosaminidase; Acid Phosphatase; Animals; Antineoplastic Agents, Alkylating; Cyclophosphamide; Edema; Female; Glomerulonephritis; Glucuronidase; Hydrolases; Injections, Intraperitoneal; Kidney; Kidney Tubules; Lysosomes; Rats; Rats, Wistar; Vacuoles

Studies were undertaken to find out the effects of low frequency pulsed electromagnetic field (PEMF) in adjuvant induced arthritis (AIA) in rats, a widely used model for screening potential therapies for rheumatoid arthritis (RA). AIA was induced by an intradermal injection of a suspension of heat killed Mycobacterium tuberculosis (500 mug/0.1 ml) into the right hind paw of male Wistar rats. This resulted in swelling, loss of body weight, increase in paw volume as well as the activity of lysosomal enzymes viz., acid phosphatase, cathepsin D, and beta-glucuronidase and significant radiological and histological changes. PEMF therapy for arthritis involved optimization of three significant factors, viz., frequency, intensity, and duration; and the waveform used is sinusoidal. The use of factorial design in lieu of conventional method resulted in the development of an ideal combination of these factors. PEMF was applied using a Fransleau-Braunbeck coil system. A magnetic field of 5 Hz x 4 muT x 90 min was found to be optimal in lowering the paw edema volume and decreasing the activity of lysosomal enzymes. Soft tissue swelling was shown to be reduced as evidenced by radiology. Histological studies confirmed reduction in inflammatory cells infiltration, hyperplasia, and hypertrophy of cells lining synovial membrane. PEMF was also shown to have a membrane stabilizing action by significantly inhibiting the rate of release of beta-glucuronidase from lysosomal rich and sub-cellular fractions. The results indicated that PEMF could be developed as a potential therapy in the treatment of arthritis in humans.

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents, Non-Steroidal; Arthritis, Experimental; Arthritis, Rheumatoid; Body Weight; Cathepsin D; Diclofenac; Edema; Electromagnetic Fields; Foot; Glucuronidase; Hindlimb; Hyperplasia; Hypertrophy; Lysosomes; Male; Mycobacterium tuberculosis; Rats; Rats, Wistar; Synovial Membrane

The anti-inflammatory activity of Salacia oblonga rootbark powder and Azima tetracantha leaf powder was assayed in male albino rats using carrageenan-induced rat paw oedema (acute inflammation) and cotton pellet granuloma (chronic inflammation) methods. Both the crude drugs were maximally active at a dose of 1000 mg/kg. In the cotton pellet granuloma assay, these drugs were able to suppress the transudative, exudative and proliferative components of chronic inflammation. Furthermore, these drugs were able to lower the lipid peroxide content of exudate and liver, gamma-glutamyl transpeptidase activity in the exudate of cotton pellet granuloma. The increased acid and alkaline phosphatase activity and decreased serum albumin in cotton pellet granulomatous rats were normalised after treatment with these drugs. It is likely that these drugs may exert their activity by antiproliferative, antioxidative and lysosomal membrane stabilization.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Anti-Inflammatory Agents; Antioxidants; Blood Chemical Analysis; Carrageenan; Disease Models, Animal; Edema; gamma-Glutamyltransferase; Gossypium; Granuloma, Foreign-Body; Lipid Peroxidation; Liver; Lysosomes; Male; Plant Extracts; Plant Leaves; Plants, Medicinal; Random Allocation; Rats; Rats, Wistar; Serum Albumin

Paraquat, a commonly used herbicide, has been shown to be toxic in exposed field workers. The objectives of this study were to (a) assess the cutaneous toxicity of paraquat in vivo in pig skin and in vitro in the isolated perfused porcine skin flap (IPPSF) and (b) quantitate its absorption in the IPPSF. The amounts of 3, 24, and 200 mg of paraquat were topically applied (5 cm2 surface area) on the ventral abdomen of pigs and biopsied after 6-8 hr for light microscopy (LM) and transmission electron microscopy (TEM). IPPSFs were topically dosed with the same concentrations and perfused for 8 hr (n = 4/treatment). The dosed area of the skin was sampled for LM, TEM, and enzyme histochemistry. IPPSFs were also treated topically with [14C]paraquat dichloride at the aforementioned concentrations (n = 4/dose) and hourly perfusate samples were collected for radiolabel determination and assessment of biochemical and physiological parameters. The epidermal changes were similar both in vivo and in vitro. The changes included epidermal intercellular edema which increased with dose and epidermal-dermal separation at the 200-mg dose. Acid phosphatase and nonspecific esterase activities were increased in the upper layers of the epidermis, while alkaline phosphatase showed a greater activity in the stratum basale layer. Glucose utilization of all treated IPPSFs was lower than that of the controls and a variation in the vascular resistance profiles was seen in all the treated flaps. Radiotracer studies indicated that a majority of the compound remained on top of the application site and minimal absorption or penetration into skin was observed. Thus, at high concentrations and prolonged exposure, paraquat may have deleterious effects on epidermal morphology in the absence of significant percutaneous absorption.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Edema; Esterases; Female; Glucose; In Vitro Techniques; Microscopy, Electron; Paraquat; Skin; Skin Absorption; Swine

This study was performed to assess the effects of misoprostol, a synthetic prostaglandin E1 analog, on cerulein-induced pancreatitis. Per group of 10 each, male Wistar rats received either cerulein (2.5 micrograms/kg/h subcutaneously), cerulein and misoprostol (500 micrograms/kg intraperitoneally at 0 and 4 h), or saline. Rats were killed 6 h after the first injection. Misoprostol treatment significantly reduced interstitial edema and acinar cell lesions induced by hyperstimulation. Pancreatic amylase and chymotrypsin contents were increased by cerulein and returned towards control levels in the misoprostol-treated group. The lysosomal volume density and the pancreatic beta-D-glucuronidase activity were significantly increased after hyperstimulation. The two parameters were significantly reduced by misoprostol. A protective effect of misoprostol against lesions induced by cerulein hyperstimulation would be a consequence of a lysosomal stabilizating effect.

Topics: Acid Phosphatase; Acute Disease; Alprostadil; Amylases; Animals; Ceruletide; Chymotrypsin; Edema; Glucuronidase; Male; Microscopy, Electron; Misoprostol; Organ Size; Pancreatic Diseases; Pancreatitis; Prostaglandins E, Synthetic; Rats; Rats, Inbred Strains

Studies were performed on mature Wistar strain rats, subjected to 43 degrees C environmental temperature for 4 h at a relative air humidity of 60-70%. Spinal cords of rats sacrificed 1, 24, 48, 72 h and one week after hyperthermia served as a material for the studies. Routinely stained preparations (H+E, Nissl) and enzymatic activity of some phosphatases and esterases was estimated as well in sections subjected to Feulgen reaction karyo- and cytophotometric measurements were performed on cell nuclei of anterior horns neurocytes, anterior columns oligodendrocytes and on anterior funicle astrocytes of the spinal cord lumbar segment. The hyperthermia resulted in rat spinal cords in several morphological and histochemical alterations. Signs of diffuse spinal cord lesion of vascular origin were present with degenerative alterations of neurocytes, oligodendroglia proliferation and astroglia hyperplasia. In histoenzymatic studies changes in enzymatic activity of NsE, AChE, ChE, AcP, ATPase and TPPase were noted. They were dependent upon the time which elapsed after hyperthermia. Karyo- and cytophotometric measurements demonstrated cell nuclei oedema in neurocytes, oligodendrocytes and astrocytes associated with a decrease in the relative DNA level and changes in density and concentration of nuclear chromatin. The observed morphological, histoenzymatic and cytophotometric changes were of a reversible type and majority of them vanished within a week after hyperthermia.

Topics: Acetylcholinesterase; Acid Anhydride Hydrolases; Acid Phosphatase; Alkaline Phosphatase; Animals; Astrocytes; Carboxylesterase; Carboxylic Ester Hydrolases; Cholinesterases; Edema; Female; Hemorrhage; Hot Temperature; Male; Neurons; Nucleotidases; Oligodendroglia; Phosphoric Monoester Hydrolases; Rats; Rats, Inbred Strains; Spinal Cord; Spinal Diseases

We describe a patient with a radiologically verified inferior vena cava obstruction due to metastatic adenocarcinoma of the prostate who was treated by orchiectomy. The prompt regression of the disease causing the obstruction confirms that orchiectomy alone can be an effective treatment of massive, functionally significant metastatic carcinoma of the prostate.

Topics: Acid Phosphatase; Adenocarcinoma; Aged; Edema; Humans; Male; Orchiectomy; Prostatic Neoplasms; Tomography, X-Ray Computed; Vascular Diseases; Vena Cava, Inferior

Studies were performed on adult rats of Wistar strain given four 7-days-spaced intraperitoneal doses of BCNU with single dose resembling to used in clinical practice. The animals were sacrificed at the seventh day after the last dose of the drug. Morphological alterations were evaluated in H + E or cresyl violet stained sections. In frozen microtome sections histoenzymatic reactions were performed to detect enzymatic activity of some phosphatases and esterases. Karyo- and cytophotometric measurements of pyramidal cell nuclei in frontal and parietal cortex and of motor neurons in trigeminal nerve nucleus were performed in sections subjected to Feulgen reaction, using automatic microscopic image analyzer "Morphoquant" (VEB Carl Zeiss, Jena). The performed studies showed that administration of multiple therapeutic doses of BCNU lead to primary injury of vascular wall as oedema and proliferation of endothelium and small perivascular haemorrhages. The cytostatic drug induced a decrease in NsE and AlkP enzymatic activities, increased activity of AChE, ChE, AcP and ATPase and topographically variable changes in intensity of TPPase enzymatic reaction. Several karyo- and cytophotometric alterations were observed also in neurocyte cell nuclei which became elongated and acquired a more round shape. This was associated with a decrease in relative DNA content, loosening of nuclear chromatin structure and with shifting chromatin lumps toward periphery of cell nuclei.

Topics: Acetylcholinesterase; Acid Phosphatase; Alkaline Phosphatase; Animals; Brain; Carmustine; Cell Nucleus; Cholinesterases; Chromatin; DNA; Edema; Esterases; Female; Hemorrhage; Male; Neurons; Phosphoric Monoester Hydrolases; Rats; Rats, Inbred Strains; Thiamine Pyrophosphatase

We employed an extravascular perfusion system through the subarachnoid space of the traumatized spinal cord of the cat for the delivery of oxygen utilizing a fluorocarbon emulsion containing essential nutrients, termed the oxygenated fluorocarbon nutrient solution (OFNS). Animals perfused for 2 hours with saline after impact injury of the spinal cord had significantly less edema at 1 cm below this site of injury than injured, untreated animals. However, in injured animals perfused with OFNS there was significant protection from spinal cord edema at both 1 and 2 cm below the site of injury. OFNS perfusion reduced the magnitude of hemorrhagic necrosis in both the gray and the white matter and protected the anterior horn cells against lysis at the site of injury. Adenosine triphosphate (ATP) is decreased within 1 minute and remains suppressed for 1 hour in gray and white matter of unperfused, injured animals. The level of ATP in both gray and white matter was significantly higher in injured OFNS-perfused animals than in saline-treated animals at the site below the spinal cord injury. Our data show that OFNS perfusion of the injured spinal cord reduced necrosis and edema and tended to normalize the levels of high energy ATP and intact anterior horn cells. These results demonstrate the feasibility of treating ischemic hypoxia of the spinal cord after trauma through an extravascular perfusion route that utilizes a fluorocarbon emulsion as a vehicle for the delivery of oxygen and other cellular nutrients.

Topics: Acid Phosphatase; Adenosine Triphosphate; Animals; Anterior Horn Cells; Cats; Edema; Female; Fluorocarbons; Male; Necrosis; Perfusion; Spinal Cord; Spinal Cord Injuries

Monoarticular arthritis in the rabbit has been used to study the effect of intra-articular administration of cortisol-21-phosphate and alpha-1-proteinase inhibitor. The preparations were administered both separately and in combination. All treatments improved parameters associated with joint biochemistry and histopathology, but the greatest effect was found when steroid was combined with anti-proteinase. Cortisol-21-phosphate had both an anti-inflammatory and anti-arthritic action, whereas alpha-1-proteinase inhibitor showed little anti-inflammatory action but had some anti-arthritic effect. Alpha-1-proteinase inhibitor had no anti-inflammatory action against carrageenan induced oedema in the rat, but was anti-arthritic against adjuvant induced arthritis in the rat where it reduced both primary and secondary arthritis.

Topics: Acid Phosphatase; alpha 1-Antitrypsin; Animals; Arthritis; Arthritis, Experimental; Blood Proteins; Disease Models, Animal; Edema; Hydrocortisone; Injections, Intra-Articular; Proteins; Rabbits; Rats; Rats, Inbred Strains; Synovial Fluid

Sterile polyester sponge-induced exudates in the rat have been investigated for high molecular weight substances with anti-inflammatory activity against carrageenan-induced oedema in the rat. The only substances found with this activity were dialysable molecules. Crude but sterile protein fractions isolated from exudate stabilized guinea-pig macrophages at low concentrations. The proteins present in exudates appeared to be identical to normal rat plasma proteins. It is concluded that anti-inflammatory activity associated with high molecular substances in exudate may have been due to bacterial contamination.

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents; Edema; Exudates and Transudates; Guinea Pigs; Immunoelectrophoresis; In Vitro Techniques; Macrophages; Peptide Hydrolases; Rabbits; Rats

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents; Arylsulfatases; Edema; Glucocorticoids; Glucuronidase; Liver; Lysosomes; Male; Protein Deficiency; Rats

Sesquiterpene lactones containing an alpha-methylene-gamma-lactone moiety were shown to be potent inhibitors of carrageenan-induced edema and chronic adjuvant-induced arthritis in rodents at 2.5 mg/kg/day. The mode of action of sesquiterpene lactones as anti-inflammatory agents appeared to be at multiple sites; for example, at 5 X 10(-4) M, the sesquiterpene lactones effectively uncoupled the oxidative phosphorylation of human polymorphonuclear neutrophils and elevated the cyclic adenosine monophosphate levels of rat neutrophils and rat and mouse liver cells. Free and total lysosomal enzymatic activity was inhibited by these agents at 5 X 10(-4) M in both rat and mouse liver and rat and human neutrophils. Furthermore, the structure-activity relationships for the stabilization of lysosomal membrane for rat liver cathepsin activity followed the same structural requirement necessary for anti-inflammatory activity; i.e., the alpha-methylene-gamma-lactone moiety contributed the most activity, whereas the beta-unsubstituted cyclopentenone and alpha-epoxycyclopentanone contributed only minor activity. Human polymorphonuclear neutrophil chemotaxis was inhibited at low concentrations (i.e., 5 X 10(-5) and 5 X10(-6) M), whereas prostaglandin synthetase activity was inhibited at a higher concentration (i.e., 10(-3) M) by the sesquiterpene lactones.

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents; Arthritis; Arylsulfatases; Cathepsins; Chemotaxis, Leukocyte; Cyclic AMP; Cyclooxygenase Inhibitors; Edema; Humans; In Vitro Techniques; Lactones; Liver; Lysosomes; Male; Mice; Neutrophils; Oxidative Phosphorylation; Rats; Sesquiterpenes; Structure-Activity Relationship; Uncoupling Agents

The non-depolymerised mucopolysaccharides of the anterior chamber angle can become hydrated. This biological oedema can obstruct the trabcculae, but the physiological liberation of catabolic enzymes from the lysosomes depolymerises the mucopolysaccharides and prevent this obstruction. This is, on the contrary, facilited by the corticosteroids, which reinforce the lysosomal membranes and impede the liberation of the catabolic enzymes. There are clones of goniocytes which are corticosensitive and other which are not. Depending upon the predominace of the one or the other, the cortisone test will be positive or negative.

Topics: Acid Phosphatase; Adrenal Cortex Hormones; Animals; Anterior Chamber; Aqueous Humor; Cells, Cultured; Edema; Fibroblasts; Glaucoma; Glycosaminoglycans; Lysosomes; Rabbits

Protease, antiprotease, and acid phosphatase blood levels of adjuvant arthritic rats were determined. The protease levels appear to vary inversely with the antiprotease levels. Changes in the protease levels correspond closely to changes in the acid phosphatase levels. Thus it is likely that the lysosomes contribute to the proteases present in the blood. Administered cortisol appears to raise blood antiprotease levels in both normal and arthritic rats and this may reflect an anti-inflammatory action by this drug.

Topics: Acid Phosphatase; alpha 1-Antitrypsin; Animals; Arthritis; Arthritis, Experimental; Clinical Enzyme Tests; Edema; Exudates and Transudates; Granulation Tissue; Hydrocortisone; Peptide Hydrolases; Protease Inhibitors; Rats

Adult white mice were continually treated by intraperitoneal injections of normal serum of various species (neat, horse, man, rabbit, mouse) for 3 hours up to 16 days. Control animals received injections of physiological saline under the same conditions. In the mouse pancreas, the repeated intraperitoneal injections of foreign serum conformably resulted in an interstitial edema, a first granulocytic and histiocytic, later on markedly lymphoplasmactyic interstitial inflammation with single dystrophic acinar cells as well as in a mild intersitial fibrosis after 8 or 16, resp., days of serum application. Histochemically, the exocrine pancreas cells showed a moderate increase in activity of adenosintriphosphatase, nonspecif esterase as well as acid and acaline phosphatase. All the changes described were most considerably pronounced after treatment with bovine serum. The interstitial pancreatitis after continual foreign serum applications regarded as the morphologie expression of a pathogenic immune phenomenon of the serum sickness type in case of a serum sickness reaction taking place preferably in the peritoneal cavity.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Blood; Cattle; Edema; Esterases; Histiocytes; Horses; Humans; Immunization; Leukocytes; Lymphocytes; Male; Mice; Pancreas; Pancreatitis; Peritoneal Cavity; Rabbits; Serum Sickness; Time Factors

Intracellular lysosomal and nonlysosomal enzymes, as well as tissue edema, were measured in spinal cords of monkeys up to 20 days following a 300 gm-cm open injury. Although edema was maximal between six hours and 11 days, enzyme elevation was delayed. Lysosomal enzyme acid cathepsin increased beginning at five days and the beta-glucuronidase and beta-glycerophosphatase increase began at 11 days. Nonlysosomal enzymes were either not elevated or showed a slight rise. These data suggest that edema, one of the secondary damaging factors in spinal injury, is not a result of release of these intracellular enzymes. Also it appears that intracellular enzymes do not participate in early secondary damaging processes in severe spinal injury.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Cathepsins; Edema; Glucuronidase; Glycerophosphates; Haplorhini; Intracellular Fluid; Lysosomes; Macaca mulatta; Peptide Hydrolases; Phosphoric Monoester Hydrolases; Spinal Cord; Spinal Cord Injuries; Time Factors

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents, Non-Steroidal; Carrageenan; Edema; Glucuronidase; Hindlimb; Male; Rats

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents; Carrageenan; Depression, Chemical; Edema; Fibroblasts; Heparin; Histocytochemistry; Lysosomes; Phenylbutazone; Rats; Sodium Salicylate

Topics: Acid Phosphatase; Animals; Aspirin; Capillary Permeability; Dactinomycin; Dose-Response Relationship, Drug; Edema; Evans Blue; Extremities; Glucuronidase; Histamine; Hydrocortisone; Indomethacin; Inflammation; Male; Rats

Topics: Acid Phosphatase; Animals; Arthus Reaction; Basement Membrane; Biopsy; Capillary Permeability; Edema; Epithelium; Fluorescent Antibody Technique; Globulins; Goats; Humans; Leukocytes; Mouth Mucosa; Rabbits; Sheep

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: Abnormalities, Drug-Induced; Acid Phosphatase; Animals; Cell Membrane; Drug Interactions; Drug Synergism; Edema; Embryo Implantation; Esters; Female; Fetal Death; Glucuronidase; Hindlimb; Inflammation; Lysosomes; Male; Methanol; Mice; Nicotinic Acids; Pregnancy; Rats; Salicylates; Stimulation, Chemical

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents; Arthritis; Bradykinin; Carrageenan; Edema; Fluorides; Foot; Glucuronidase; Hindlimb; Lethal Dose 50; Liver; Lysosomes; Male; Rats; Rats, Inbred Strains; Serotonin; Triamcinolone Acetonide

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Anti-Inflammatory Agents; Aspirin; Betamethasone; Carrageenan; Dexamethasone; Edema; Female; Glucuronidase; Hexosaminidases; Indomethacin; Inflammation; Lysosomes; Methotrexate; Nystatin; Phenylbutazone; Prednisolone; Rats; Time Factors

Topics: Acid Phosphatase; Amino Acids; Animals; Capillary Permeability; Cyclohexanecarboxylic Acids; Depression, Chemical; Edema; Glucuronidase; Guinea Pigs; Hindlimb; Lysosomes; Methylamines; Muscles; Organ Size; Wounds and Injuries

Topics: Acid Phosphatase; Aminocaproates; Animals; Antifibrinolytic Agents; Aprotinin; Carbon Tetrachloride Poisoning; Chymotrypsin; Cyclohexanecarboxylic Acids; Edema; Female; Fibrinolysin; Guinea Pigs; Inflammation; Kallikreins; Microbial Collagenase; Pancreatic Elastase; Peptides; Protease Inhibitors; Rats; Ribonucleases; Trypsin

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Aortic Diseases; Edema; Enzymes; Esterases; Glucosephosphate Dehydrogenase; Glycosaminoglycans; Histocytochemistry; Hypertension; Lipase; Nucleotidases; Rabbits; Sulfatases

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; Brain; Brain Diseases; Cerebrospinal Fluid; DNA; Edema; Histocytochemistry; Kidney Diseases; Mercury Poisoning; Phosphoric Monoester Hydrolases; Rabbits; Research; RNA; Toxicology