acid-phosphatase and Hemolysis

Acetone may induce oxidative stress leading to disturbance of the biochemical and physiological functions of red blood cells (RBCs) thereby affecting membrane integrity. Vitamin E (vit E) is believed to function as an antioxidant in vivo protecting membranes from lipid peroxidation. The aim of the present study was the evaluation of possible protective effects of vit E treatment against acetone-induced oxidative stress in rat RBCs. Thirty healthy male Wistar albino rats, weighing 200-230 g and averaging 12 weeks old were randomly allotted into one of three experimental groups: Control (A), acetone-treated (B) and acetone + vit E-treated groups (C), each containing ten animals. Group A received only drinking water. Acetone, 5% (v/v), was given with drinking water to B and C groups. In addition, C group received vit E dose of 200 mg/kg/day i.m. The experiment continued for 10 days. At the end of the 10th day, the blood samples were obtained for biochemical and morphological investigation. Acetone treatment resulted in RBC membrane destruction and hemolysis, increased thiobarbituric acid reactive substance (TBARS) levels in plasma and RBC, and decreased RBC vit E levels. Vit E treatment decreased elevated TBARS levels in plasma and RBC and also increased reduced RBC vit E levels, and prevented RBC membrane destruction and hemolysis. In conclusion, vit E treatment appears to be beneficial in preventing acetone-induced oxidative RBC damage, and therefore, it can improve RBC rheology.

Topics: Acetone; Acid Phosphatase; Animals; Aspartate Aminotransferases; Erythrocyte Count; Erythrocytes; Hemolysis; L-Lactate Dehydrogenase; Male; Oxidative Stress; Rats; Rats, Wistar; Thiobarbituric Acid Reactive Substances; Vitamin E

The effect of zinc exposure on some properties of the carp erythrocyte membrane was studied in vitro. Red blood cells plasma membranes were separated from other cellular membranes using a combination of differential and density gradient centrifugation. The purity of obtained plasma membrane preparations was determined by measuring the activity of the marker enzymes. Electrophoretic patterns of the main erythrocyte membrane proteins excluded their degradation during the isolation and purification procedure. Carp erythrocyte membranes, obtained from cells previously incubated with increasing ZnSO4 concentrations, were used to elucidate the effect of zinc ions on their physical and biochemical properties. Using fluorescent probes: 12-AS and TMA-DPH, we found that zinc ions reduced the fluidity of the lipid bilayer, both in the middle and near the aqueous interface. Moreover, it was observed that zinc had no significant influence neither on the Na,K-ATPase activity nor on the thiol groups content in the erythrocyte membrane. We also detected that incubation of erythrocytes with zinc lead to the marked decrease of hemolytic resistance of the cells. Our studies demonstrate that zinc at higher concentrations may be toxic to carp erythrocytes causing changes in the membrane fluidity and hemolytic resistance.

Topics: Acid Phosphatase; Animals; Carps; Catalase; Cell Fractionation; Electrophoresis, Polyacrylamide Gel; Erythrocyte Membrane; Fluorescent Dyes; Hemolysis; In Vitro Techniques; Lipid Bilayers; Membrane Fluidity; Nucleic Acids; Sodium-Potassium-Exchanging ATPase; Succinate Dehydrogenase; Sulfhydryl Compounds; Zinc

We describe an improved method for the kinetic measurement of tartrate-resistant acid phosphatase (TrACP; EC 3.1.3.2) activity in serum. Of the TrACP derived from erythrocytes, platelets, and macrophages (osteoclasts and others), that from the first two sources is also resistant to fluoride, whereas skeletal TrACP is sensitive to fluoride. Thus, osteoclast-derived TrACP can be measured specifically by exploiting its sensitivity to fluoride. We measured the activity of tartrate-resistant and fluoride-sensitive acid phosphatase (TrFsACP) by using 2,6-dichloro-4-acetylphenyl phosphate as substrate at pH 6.2. The activity of TrFsACP in serum was increased by adding hexadimethrine bromide (Polybrene) to the reaction mixture. This method was not influenced by hemolysis with hemoglobin concentrations as great as 0.9 g/L. The mean +/- SD values of TrFsACP activity by this method were 20.4 +/- 2.8 and 16.4 +/- 2.3 U/L for young (ages 20-29 years) men (n = 34) and women (n = 50), respectively. The highest mean TrFsACP activity was found among children younger than 15 years, followed by that in elderly subjects (older than 60).

Topics: Acid Phosphatase; Adult; Animals; Blood Platelets; Cattle; Enzyme Inhibitors; Erythrocytes; Female; Hemolysis; Heparin; Heparin Antagonists; Hexadimethrine Bromide; Humans; Isoenzymes; Kinetics; Male; Organophosphates; Osteoclasts; Sodium Fluoride; Tartrate-Resistant Acid Phosphatase; Tartrates

The present study was undertaken to investigate the capacity to generate reducing equivalents in erythrocytes from experimentally copper-poisoned sheep. Ten ewes were dosed orally with CuSO4 to induce the Cu toxicity. Copper dosing was stopped at the first day of hemolysis. The activity of glucose-6-phosphate dehydrogenase (G6PD) in the erythrocytes, the levels of reduced glutathione (GSH) and glucose (in serum and erythrocytes) was examined at frequent intervals. The copper-poisoned sheep had reduced levels (25-35% less) of glucose in serum and erythrocytes than controls. The activity of G6PD in erythrocytes from sheep was 50-60% of typical levels found in human erythrocytes. Immediately before the hemolytic period, the copper-poisoned sheep showed decreased activity of G6PD, declining to 65% of the initial activity. In addition, we found decreased blood levels of reduced GSH in copper-poisoned sheep. There appears to be a relationship between decreased capacity to generate reducing equivalents and the overload of copper in sheep erythrocytes.

Topics: Acid Phosphatase; Animals; Antioxidants; Blood Glucose; Copper; Erythrocytes; Female; Glucosephosphate Dehydrogenase; Glutathione; Hemolysis; Humans; Sheep

A specific ampholine mixture resulted in appreciable enhancement of discriminating features in electrophoregrams of 6 common ACP phenotypes, thus allowing unequivocal interpretation of the enzyme types in fresh blood and in bloodstains. The employed procedure resulted in marked increase in the limit of ACP phenotype detectability in bloodstains and substantial enhancement of sensitivity and efficacy of the analysis. PhastIEF appeared useful in ACP phenotyping due to its reproducibility and duration of separation. In the case of some ACP phenotypes in ageing bloodstains this technique allows even longer detectability limits compared to PAGE IEF.

Topics: Acid Phosphatase; Blood Stains; Electrophoresis; Erythrocytes; Hemolysis; Humans; Isoenzymes; Phenotype; Polymorphism, Genetic; Reproducibility of Results

A detailed investigation on the anti-inflammatory activity of the butanol fraction of a methanol extract (BMEL) of the defatted leaves of Paederia foetida was undertaken to find the pharmacological basis for the ethnomedical use of the plant. This fraction produced a significant inhibition of granulation tissue formation in cotton-pellet implanted rats. It decreased liver aspartate transaminase activity without affecting serum aspartate transaminase activity. It did not, however, affect adrenal weight and ascorbic acid content significantly, thus ruling out a stimulation of the adrenal-pituitary axis. BMEL antagonised hyposaline-induced haemolysis of human red blood cells and an elevation of rat serum acid phosphatase activity, indicating the presence of a membrane stabilising activity. It also inhibited the elevation of serum orosomucoid levels in rats, suggesting the possibility of the presence of disease-modifying antirheumatic activity. The results indicate that there is some rationale behind the ethnomedical use of the plant for treating inflammatory disorders.

Topics: 1-Butanol; Acid Phosphatase; Adrenal Glands; Animals; Anti-Inflammatory Agents; Ascorbic Acid; Aspartate Aminotransferases; Blood Proteins; Butanols; Chemical Fractionation; Disease Models, Animal; Erythrocyte Membrane; Female; Granuloma; Hemolysis; Humans; Liver; Male; Medicine, Traditional; Methanol; Organ Size; Orosomucoid; Plant Extracts; Rats; Spleen

Clinical chemists frequently encounter hemolyzed samples. Our study examines the effects of hemolysis on the results of 25 common biochemical tests. We collected 60 15-mL blood samples from inpatients and outpatients and mechanically hemolyzed 10 mL of the samples in a two-step procedure. We classified serum from these samples as being nonhemolyzed, moderately hemolyzed, or severely hemolyzed and then performed 25 common biochemical tests. Statistical analysis of the results showed that hemolysis had the greatest effect on the lactate dehydrogenase, acid phosphatase, and potassium tests.

Topics: Acid Phosphatase; Blood Chemical Analysis; False Positive Reactions; Hemolysis; Humans; L-Lactate Dehydrogenase; Potassium

Topics: Acid Phosphatase; Blood Platelets; Blood Preservation; Cell Separation; Erythrocyte Aging; Erythrocytes; Hemolysis; Histamine; Humans; Leukocyte Elastase; Leukocytes; Pancreatic Elastase; Serotonin; Time Factors

Quantitatively much higher Concanavalin A (Con. A) agglutinability, haemolytic potency, and activities of acid hydrolases, namely phosphatase (EC 3.1.3.2), ribonuclease (EC 2.7.7.16), deoxyribonuclease (EC 3.1.4.5) and proteinase--were observed in a virulent strain of Entamoeba histolytica (IP-106), as compared to attenuated and avirulent strains (200-NIH) and DKB respectively. In addition, significant differences in these parameters were observed among clonal cultures derived from the latter two cultures by cultivation of single amoebic cells picked out by micromanipulation. Repeated sub-culturing of parent cultures of both these strains in cholesterol-enriched medium resulted in marked enhancement of all the above activities, but no such change occurred in the derived clonal cultures following similar cholesterol treatment. The implication of these findings in relation to enhancement of the virulence of E. histolytica by cholesterol is discussed.

Topics: Acid Phosphatase; Agglutination; Animals; Cholesterol; Concanavalin A; Culture Media; Deoxyribonucleases; Endopeptidases; Entamoeba histolytica; Hemolysis; Ribonucleases; Virulence

Eighteen ewes in two groups were dosed orally with CuSO4 to induce chronic Cu toxicity. Copper dosing was stopped at the first rise of acid AP activity in the serum in group 1 sheep and on the first day of haemolysis in group 2 sheep. Liver samples were obtained 1 week prior to the start of Cu dosing, at the first rise of acid phosphatase (AP) activity in serum and on the first day of haemolysis. These liver samples were homogenized and were separated into nuclear (N), heavy mitochondrial (MH), light mitochondrial (ML), microsomal (MI) and cytosolic (CY) fractions by centrifugation. The Cu concentration and specific activities of AP were determined in the liver, LH and subcellular fractions. The composition of the fractions was studied by light and electron microscopy. In the predosing biopsies, the concentration and percentage of Cu and the total specific activity of AP were highest in the ML fractions. With increasing Cu loading, the concentration of Cu in all fractions increased; the percentage of Cu increased in the N and MH fractions, decreased in the ML and MI fractions and was maintained at a constant level in the CY fractions. The total specific activities of AP in LH, N, MH, MI and CY fractions were increased and the activity was highest in the MH fraction. The results indicate that the increase in the concentration of Cu in liver cells was predominantly in lysosomes and cytosol. Furthermore, it is suggested that the necrosis of isolated hepatocytes observed in chronic Cu-poisoned sheep may be due to a saturation of the uptake of Cu into the lysosomal system of the cell, leading to the accumulation of toxic levels of Cu in the cytosol.

Topics: Acid Phosphatase; Animals; Centrifugation; Copper; Cytosol; Female; Hemolysis; Liver; Lysosomes; Microscopy, Electron; Microsomes, Liver; Mitochondria, Liver; Sheep; Sheep Diseases; Subcellular Fractions

The maturation of reticulocytes into erythrocytes was demonstrated in vitro. Reticulocytosis was induced in rats by repeated bleeding or by phenylhydrazine injections. Whole blood samples were then incubated for 2 days at 37 degrees C. Reticulocytes in culture changed from polylobulated, monoconcave or triconcave forms to biconcave disks. During the first 12 h in vitro, the average reticulocyte count decreased from 39% to 12%, and the membrane-bound organelles, ribosomes and exocytic figures in the remaining reticulocytes were markedly diminished. In contrast, the number of red cells containing inclusions of denatured haemoglobin (Heinz bodies) in phenylhydrazine-treated blood did not decline. The reduction in reticulocyte count was not the result of differential cell destruction, since little haemolysis occurred in vitro. During red cell maturation three modes of organelle removal were observed particularly well when mitochondria were followed by cytochrome oxidase cytochemistry. First, some mitochondria degenerated, presumably through autolysis, by swelling, losing cristae and forming small single membrane-bound vesicles. Second, individual mitochondria became enclosed in vacuoles that fused with the plasma membrane and expelled their mitochondria by exocytosis. Third, autophagic vacuoles containing mitochondria, cytosol and membrane fragments fused with existing lysosomes. We conclude that all aspects of normal reticulocyte maturation occur in vitro, independent of the spleen, including the removal of organelles and the assumption of the mature biconcave disk shape.

Topics: Acid Phosphatase; Animals; Cells, Cultured; Electron Transport Complex IV; Erythrocyte Count; Erythropoiesis; Exocytosis; Heinz Bodies; Hematocrit; Hemolysis; Hydrogen-Ion Concentration; Microscopy, Electron; Phenylhydrazines; Rats; Rats, Inbred Lew; Rats, Inbred WF; Reticulocytes

Topics: Acid Phosphatase; Alcoholism; Anemia; Bone Marrow Cells; Erythrocyte Indices; Erythropoiesis; Female; Fetal Alcohol Spectrum Disorders; Folic Acid Deficiency; Hemolysis; Humans; Megaloblasts; Mitochondrial Swelling; Naphthol AS D Esterase; Pregnancy; Pyridoxal Phosphate

Physicochemical properties and systemic effects of the enterotoxin of Klebsiella pneumoniae has been studied. The enterotoxin had a molecular weight between 10 000 to 50 000. It was protein in nature, and heat and acid stable, inducing a dilatatory response in the gut. It haemolyzed the erythrocytes of various animals including man. It had a capillary permeability activity. In addition, when administered parenterally it increased the level of blood glucose, serum cholesterol, serum alkaline phosphatase and serum acid phosphatase.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Bacterial Proteins; Blood Glucose; Capillary Permeability; Cholesterol; Enterotoxins; Hemolysis; Hot Temperature; Hydrogen-Ion Concentration; Klebsiella pneumoniae; Molecular Weight; Rabbits

Topics: Acid Phosphatase; Adenosine Diphosphate; Animals; Blood Cell Count; Blood Coagulation; Blood Platelets; Dogs; Hemolysis; Heparin; Platelet Aggregation; Platelet Factor 3; Stress, Mechanical

In trophoblastic epithelial cells of the sheep placenta the breakdown of erythrocytes within complex erythrolysosomes was studied at the ultrastructural level. It was found that the formation of complex erythrolysosomes containing from two to several erythrocytes as a result of fusion of erythrolysosomes within the epithelial cells was a common occurrence when the epithelial cells engulfed a large number of erythrocytes. The erythrocytes enclosed in complex erythrolysosomes appear to be either in the same or in different stages of hemolysis. In the process of breakdown of erythrocytes within complex erythrolysosomes five successive stages of hemolysis could be distinguished. Acid phosphatase activity was demonstrated in the complex erythrolysosomes and appeared to be located in the angular interspaces between the erythrocytes and the lysosomal membrane. The fragmentation of complex erythrolysosomes with formation of small hemoglobin-containing lysosomes also occurred. The fusion of erythrolysosomes with formation of complex erythrolysosomes can be considered as an additional mechanism in the process of erythrocyte breakdown in the epithelial cells of the sheep placenta.

Topics: Acid Phosphatase; Animals; Epithelium; Erythrocytes; Female; Hemolysis; Lysosomes; Pregnancy; Sheep; Trophoblasts

A prospective study was done to evaluate 47 patients with early stage prostatic cancer. Pelvic lymphadenectomy was combined with bone marrow acid phosphatase determination to evaluate early metastatic disease. Thirteen patients (28 per cent) had tumor in the pelvic lymph nodes. In no instance was the bone marrow acid phosphatase elevated to more than the normal value for serum by the substrate used. Combined high grade and stage tumors seemed to have an increased incidence of metastases to pelvic lymph nodes. A surprisingly high incidence of B1 lesions (5 of 21 patients or 24 per cent) had positive lymph nodes. Generally, the nodes were moderately well or well differentiated lesions. The metastases were unilateral, frequently microscopic only and involved 1 or only a few nodes. Pelvic lymphadenectomy seems to have a well defined role in the diagnostic study of early stage prostatic cancer, while bone marrow acid phosphatase determinations were of no value.

Topics: Acid Phosphatase; Adenocarcinoma; Aged; Biopsy, Needle; Bone Marrow; Hemolysis; Humans; Isoenzymes; L-Lactate Dehydrogenase; Lymph Node Excision; Lymph Nodes; Lymphatic Metastasis; Male; Middle Aged; Pelvis; Prospective Studies; Prostatic Neoplasms

Hemolysis in serum specimens is commonplace. This study examines the effect of hemolysis on results of selected chemical assays. Hemolysis was simulated by adding hemolysate to serum to give hemoglobin concentrations of 90 to 2800 mg/liter and a rating by technologists of 0 to 4 + hemolyzed. The effect of hemolysis on values for some serum constituents, particularly acid phosphatase and creatine kinase, was shown to be method dependent. Not unexpectedly, hemolysis most affects results for lactate dehydrogenase.

Topics: Acid Phosphatase; Aspartate Aminotransferases; Bicarbonates; Blood Chemical Analysis; Creatine Kinase; Hemoglobinometry; Hemolysis; Humans; Iron; L-Lactate Dehydrogenase; Potassium

The levels of total and l-tartrate labile acid phosphatase were studied in 49 patients with prostatic carcinoma. The results were compared with the results from a control group. The acid phosphatase levels from the bone marrow were above the upper normal limit of serum acid phosphatase both in the control group and in patients with prostatic carcinoma. This may be due to acid phosphatase released from blood cells during haemolysis. There was a positive correlation between serum and bone marrow acid phosphatase levels in patients with prostatic carcinoma. Significantly raised levels of bone marrow acid phosphatase (above the upper limit of the normal range from the control group) were observed only in advanced stage IV patients with significantly increased serum levels. The levels of bone marrow acid phosphatase gave no supplementary diagnostic information in any of the patients with prostatic carcinoma. Doubt is expressed concerning the hypothesis that raised levels of bone marrow acid phosphatase are diagnostic of early metastases from prostatic carcinoma.

Topics: Acid Phosphatase; Bone Marrow; Bone Neoplasms; Hemolysis; Humans; Male; Prostatic Neoplasms

Mycobactericidal activity of long-chain fatty acids was confirmed by in vitro exposure of BCG. The killing effect was accompanied by inhibition of the membrane-bound acid phosphatase activity. Such active fatty acids were those having a stronger hemolytic activity (e.g., C12:0, C14:0, C18:1, C18:2). Heat-killed BCG cells or their cell walls adsorbed the toxic fatty acids, whereas the fatty acid-insensitive E. coli cells did not. It was suggested that the mycobactericidal action of long-chain fatty acids is due to their detergent-like action on the cytoplasmic membrane, and that the determinant factor for the fatty acid-sensitivitiy of bacteria is the property of the cell wall by which fatty acids are adsorbed so that the active site is brought into contact with the inner membrane.

Topics: Acid Phosphatase; Cell Membrane; Detergents; Erythrocytes; Fatty Acids; Hemolysis; Mycobacterium bovis; Oleic Acids; Structure-Activity Relationship; Temperature; Time Factors

Topics: Acid Phosphatase; Animals; Cell Membrane; Freezing; Hemolysis; Histocytochemistry; Mitochondria; Rabbits; Reticulocytes; Vacuoles

Experiments were carried out to determine the effectiveness of steroid therapy in vitamin E-deficiency, as measured by autohemolysis of isolated RBC's body weight gain, serum creatine phosphokinase activity, and stabilization or labilization of isolated hepatic lysosomes. Results of such experiments would indicate whether triamcinolone acetonide could supplant vitamin E in vitamin E-deficiency states via its ability to stablize various membranes. Autohemolysis induced by vitamin E-deficiency could not be prevented by daily administration of triamcinolone. Daily dosages of 0.1 and 0.4 mg/kg (ip) triamcinolone given concomitantly with replacement vitamin E (at sufficient dosages to reverse the autohemolysis) resulted in an increased autohemolysis. No changes in lysosomal membrane fragility were noted when hepatic lysosomes were obtained from vitamin E-deficient rats with triamcinolone resulted in a greater attenuation of body-weight gain. Creatine phosphokinase levels were not augmented in vitamin E-deficient rats. Vitamin E-deficient rats supplemented with vitamin E and treated with triamcinolone, manifested an increase in creatine, phosphokinase. It was therefore concluded that although triamcinolone and vitamin E possess a common ability to stablize membranes and proteins, their mechanisms must be different since triamcinolone could not substitute for vitamin E in a deficiency state. Indeed, triamcinolone was found to be more toxic in the absence of vitamin E.

Topics: Acid Phosphatase; Animals; Body Weight; Creatine Kinase; Drug Evaluation, Preclinical; Eating; Glucuronidase; Hemolysis; In Vitro Techniques; Liver; Lysosomes; Male; Rats; Triamcinolone Acetonide; Vitamin E Deficiency

For studies on the lysosome-stabilizing effect of D-glucaric acid derivatives which have been found to have anti-inflammatory effect, the available and soluble enzyme activities of acid phosphatase of rat liver lysosomes were determined. Saliployed as standards. Lysosomes were incubated with drugs under specific conditions which allowed the data on the stabilizing activity of the drugs to be reproducible. The inhibitory effect of D-glucaro-1, 4-lactone, salicylic acid and phenylbutazone onover a wide range of concentrations. D-glucaro-1, 4-lactone as well as salicylic acid exhibited concentration-dependent lysosome-stabilizing effect whereas phenlybutazone had an optimum concentration for its lysosome-stabilizing effect. In addition, D-glucaro-1, 4-lactone,saliclicacid and phenylubtazone were also examined for their effects on heat-induced and saponin-induced hemolysis of rat erythrocyres. Both salicylic acid and phenylbutazone exhibited potent stabilziing and labilizing effects on heat-induced and saponin-induced hemolysis of eryhthrocytes, respectively. D-glucaro-1, 4-lactone, however, was incabale of affecting the hemolysis of erythrocytes. There appears to be a difference in the mechanism of the lysosome-stabilizing effects between D-glucaric acid derivatives and other anti-inflammatory drugs.

Topics: Acid Phosphatase; Adipates; Animals; Anti-Inflammatory Agents; Dose-Response Relationship, Drug; Erythrocytes; Ethanol; Hemolysis; In Vitro Techniques; Liver; Lysosomes; Male; Monosaccharides; Phenylbutazone; Rats; Salicylates; Saponins; Sucrose; Sugar Acids

Topics: Acid Phosphatase; Adult; Bone Marrow; Erythrocytes; Hematocrit; Hemoglobinopathies; Hemoglobins, Abnormal; Hemolysis; Humans; Iron; Iron Radioisotopes; Male; Syndrome; Transferrin

Cytotoxicity and hemolysis were studied in chrysotile and quartz. The biological activity of the surface seemed to be different between chrysotile and quartz. Quartz lost its cytotoxicity on heating over about 500 degrees C. However chrysotile showed remarkable toxicity and induced hemolysis on heating between 650 and 800 degrees C, compared with the original unheated specimens. The mice injected intraperitoneally with minerals heated in this temperature range generally died within 48 hr after injection, while those injected with untreated chrysotile or chrysotile heated in the other heat ranges did not. The products in this range were highly disorded materials. It was assumed that the change of biological effects resulting from heat treatment may be related to the disordered state of chrysotile in the process of transformation into forsterite. The relationship between chemical character and cytotoxicity of the heated chrysotile specimens was also studied.

Topics: Acid Phosphatase; Alkalies; Animals; Asbestos; Body Weight; Erythrocytes; Hemolysis; Hot Temperature; Hydrogen-Ion Concentration; Lactates; Macrophages; Mice; Quartz; Serum Albumin, Bovine

Topics: Acclimatization; Acid Phosphatase; Adenosine Triphosphate; Animals; Body Temperature; Chlorpromazine; Cold Temperature; Diet; Dose-Response Relationship, Drug; Enzyme Induction; Erythrocytes; Hemolysis; Liver; Lysosomes; Malate Dehydrogenase; Membranes; Mitochondria, Liver; Phenothiazines; Subcellular Fractions; Temperature; Time Factors

Topics: Acid Phosphatase; Animals; Cell-Free System; Chloroquine; Dithiothreitol; Edetic Acid; Erythrocytes; Female; Hemoglobins; Hemolysis; Hydrogen-Ion Concentration; Malaria; Mice; Mice, Inbred BALB C; Peptide Hydrolases; Plasmodium berghei; Primaquine; Quinacrine; Rats; Solubility; Surface-Active Agents; Ultracentrifugation

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; Chondrocalcinosis; Diphosphates; Female; Gout; Hemolysis; Humans; Inflammation; Leukocytes; Lysosomes; Male; Membranes; Phagocytosis; Sex Factors; Silicon Dioxide; Uric Acid

Topics: Acid Phosphatase; Animals; Bacteriological Techniques; Coagulase; Deoxyribonucleases; Evaluation Studies as Topic; Fermentation; Hemolysis; Indoles; Mannitol; Microbial Sensitivity Tests; Nitrophenols; Organophosphorus Compounds; Penicillinase; Penicillins; Phenols; Pigments, Biological; Rabbits; Sheep; Spectrum Analysis; Staphylococcus

Topics: Acid Phosphatase; Animals; Bird Diseases; Birds; Cytoplasmic Granules; Digestion; Endoplasmic Reticulum; Female; Golgi Apparatus; Hemoglobins; Hemolysis; Hemosiderin; Histocytochemistry; Intestines; Lysosomes; Microscopy, Electron; Nematoda; Nematode Infections

Topics: Acid Phosphatase; Animals; Electrophoresis, Starch Gel; Erythrocytes; Hemolysis; Phenotype; Swine

Topics: Acid Phosphatase; Animals; Cholesterol; Chromates; Erythrocytes; Estradiol; Female; Glucuronidase; Gout; Hemolysis; Humans; Leukocytes; Liposomes; Liver; Lysosomes; Male; Muramidase; Rabbits; Silicon Dioxide; Sucrose; Sulfatases; Testosterone; Uric Acid

Topics: Acid Phosphatase; Adenosine Triphosphatases; Blood Protein Electrophoresis; Carbohydrate Epimerases; Cell Membrane; Cell Survival; Chromium Isotopes; Elliptocytosis, Hereditary; Erythrocytes; Female; Fructose-Bisphosphate Aldolase; Glucosephosphate Dehydrogenase; Glutathione; Glutathione Reductase; Glyceraldehyde-3-Phosphate Dehydrogenases; Hemoglobinometry; Hemolysis; Hexokinase; Humans; L-Lactate Dehydrogenase; Male; NADP; Phenylhydrazines; Phosphofructokinase-1; Phosphopyruvate Hydratase; Pyruvate Kinase

Topics: Acid Phosphatase; Adjuvants, Immunologic; Animals; Arthritis; Cell Membrane; Erythrocytes; Foot; Glucuronidase; Hemolysis; Hindlimb; Indomethacin; Liver; Lysosomes; Mycobacterium tuberculosis; Osmotic Fragility; Paramethasone; Phenylbutazone; Rats; Time Factors

Topics: Acid Phosphatase; Erythrocytes; Favism; Hemolysis; Humans; Infant, Newborn; Jaundice, Neonatal; Phenotype; Polymorphism, Genetic

The hydrolysis of adenosine 3'-monophosphate by serum acid phosphatase has been coupled to the liberation of ammonia from the adenosine generated through the action of exogenous adenosine deaminase. The ammonia is measured at the end of the incubation by a modification of the phenol-hypochlorite reaction of Berthelot. Optimum conditions for the enzyme reaction have been defined. Inhibition of the Berthelot reaction by the serum used in the assay is small, and may be compensated by a correction factor. Although the value for the control is high in relation to the test over the normal range, this is largely outweighed by the good sensitivity and precision of the method. The substrate is not significantly hydrolysed by erythrocyte acid phosphatase within the limits encountered in haemolysed sera. Experience of the method in routine hospital diagnosis compared favorably with that of a standard method employing disodium phenyl phosphate as substrate. It is suggested that activities greater than 3.1 IU/l should be further investigated and those greater than 3.7 IU/l should be regarded as definitely raised. The stability of human serum AcPase when promptly separated and held at 4 degrees C or - 20 degrees C was confirmed. At room temperature, acidification to pH 6.0 greatly improved stability.

Topics: Acid Phosphatase; Adenine Nucleotides; Adenosine Monophosphate; Aminohydrolases; Ammonia; Clinical Enzyme Tests; Colorimetry; Female; Hemolysis; Humans; Hydrogen-Ion Concentration; Hydrolysis; Male; Methods; Phenols; Prostatic Hyperplasia; Prostatic Neoplasms; Temperature

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: Acetylcholinesterase; Acid Phosphatase; Adenosine Triphosphatases; Bicarbonates; Calcium; Cell Membrane; Cell Membrane Permeability; Erythrocytes; Hemolysis; Humans; Hypotonic Solutions; Leucyl Aminopeptidase; Magnesium; Microscopy, Electron; Phosphorus Isotopes; Potassium; Sodium; Surface-Active Agents; Vibration

Topics: Acid Phosphatase; Animals; Anura; Digestion; Ecology; Esophagus; Esterases; Hemolysis; Hemosiderin; Histocytochemistry; Histological Techniques; Intestines; Microscopy, Electron; Nematoda

Topics: Acid Phosphatase; Animals; Birds; Digestion; DNA; Ecology; Esophagus; Esterases; Hemolysis; Histocytochemistry; Intestines; Leucyl Aminopeptidase; Microscopy, Electron; Nematoda

Topics: Acetates; Acid Phosphatase; Alkaline Phosphatase; Blood Protein Electrophoresis; Buffers; Chemistry, Clinical; Chromatography, Thin Layer; Citrates; Electrophoresis; Erythrocytes; Hemolysis; Humans; Hydrogen-Ion Concentration; Isoenzymes; Phosphoric Monoester Hydrolases; Tartrates

Topics: Acid Phosphatase; Alkalies; Animals; Carbon Radioisotopes; Dust; Hemolysis; Hot Temperature; Immune Sera; Lactates; Leucine; Macrophages; Minerals; Particle Size; Rats; Silicon Dioxide

Topics: Acid Phosphatase; Arthritis, Infectious; Arthritis, Reactive; Arthritis, Rheumatoid; Complement Fixation Tests; Complement System Proteins; Fluorescent Antibody Technique; Glucuronidase; Gout; Hemolysis; Humans; Proteins; Synovial Fluid

Topics: Acid Phosphatase; Analgesics; Animals; Anti-Inflammatory Agents; Antibody Formation; Aspirin; Blood Platelets; Blood Proteins; Cell Aggregation; Cyclophosphamide; Depression, Chemical; Fibrinolysis; Flufenamic Acid; Glucuronidase; Guinea Pigs; Hemolysis; Hydrocortisone; Indomethacin; Inflammation; Male; Mefenamic Acid; Mice; Phenylbutazone; Protein Binding; Protein Denaturation; Pyridines; Rabbits; Rats; Stimulation, Chemical

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Bile Acids and Salts; Glycerol; Hemoglobins; Hemoglobinuria; Hemolysis; Histocytochemistry; Histological Techniques; Injections, Intravenous; Injections, Subcutaneous; Kidney; Kidney Diseases; Kidney Function Tests; Kidney Tubules; Male; Rats

Topics: Acid Phosphatase; Animals; Anti-Inflammatory Agents; Biological Assay; Blood Platelets; Calcium; Erythrocytes; Hemolysis; Hot Temperature; Hypotonic Solutions; In Vitro Techniques; Indomethacin; L-Lactate Dehydrogenase; Methods; Phenylbutazone; Rats; Thrombin; Time Factors

Topics: Acid Phosphatase; Animals; Cell Membrane; Depression, Chemical; Erythrocytes; Fluorides; Hemolysis; Hydrogen-Ion Concentration; Magnesium; Nucleotides; Ouabain; Phosphates; Phosphotransferases; Potassium; Rabbits; Reticulocytes; Sodium; Solubility

Topics: Acid Phosphatase; Animals; Bacterial Proteins; Bacteriophage Typing; Culture Media; Drug Resistance, Microbial; Hemolysis; Lipids; Mice; Oxidoreductases; Oxygen Consumption; Pigments, Biological; RNA; Staphylococcal Infections; Staphylococcus; Succinate Dehydrogenase; Virulence

Topics: Acid Phosphatase; Animals; Chromatography; Chromatography, Gel; Erythrocytes; Glyceric Acids; Hemolysis; Hydrogen-Ion Concentration; Hypoxanthines; NAD; Nucleosides; Nucleotides; Phosphates; Phosphorus; Rabbits

Topics: Acid Phosphatase; Dust; Erythrocytes; Hemolysis; Humans; In Vitro Techniques; Silicon Dioxide

Topics: Acid Phosphatase; Cytoplasmic Granules; Glucuronidase; Hematology; Hemolysis; Heparin; Humans; In Vitro Techniques; Leukocyte Count; Leukocytes; Lymphocytes; Lysosomes; Phagocytosis

Topics: Acid Phosphatase; Animals; Carcinogens; Cell Membrane; Cold Temperature; Croton Oil; Erythrocytes; Esters; Glucuronidase; Hemolysis; In Vitro Techniques; Liver; Lysosomes; Malate Dehydrogenase; Male; Membranes, Artificial; Mice; Mitochondria, Liver; Nicotiana; Plant Extracts; Plants, Toxic; Rabbits; Sulfatases; Surface-Active Agents; Time Factors

Topics: Acid Phosphatase; Animals; Blood Cell Count; Blood Platelets; Cell Membrane Permeability; Dogs; Erythrocyte Aging; Erythrocytes; Extracorporeal Circulation; Hematocrit; Hemoglobinometry; Hemolysis; In Vitro Techniques; L-Lactate Dehydrogenase; Leukocyte Count; Osmotic Fragility; Potassium; Sodium

Topics: Acetylcholinesterase; Acid Phosphatase; Animals; Cell Membrane; Detergents; Erythrocytes; Hemolysis; Kinetics; N-Glycosyl Hydrolases; Potassium Chloride; Rabbits; Trypsin

Topics: Acid Phosphatase; Adolescent; Adult; Aged; Aging; Alanine Transaminase; Aspartate Aminotransferases; Blood Platelets; Erythrocytes; Female; Hemolysis; Humans; Leukocytes; Male

Topics: Acid Phosphatase; Biomedical Research; Blood Chemical Analysis; Castration; Estrogens; Hemolysis; Humans; Male; Orchiectomy; Periodicity; Physiology; Prostatic Neoplasms; Testis; Urine

Bernheimer, Alan W. (New York University School of Medicine, New York), and Lois L. Schwartz. Lysosomal disruption by bacterial toxins. J. Bacteriol. 87:1100-1104. 1964.-Seventeen bacterial toxins were examined for capacity (i) to disrupt rabbit leukocyte lysosomes as indicated by decrease in turbidity of lysosomal suspensions, and (ii) to alter rabbit liver lysosomes as measured by release of beta-glucuronidase and acid phosphatase. Staphylococcal alpha-toxin, Clostridium perfringens alpha-toxin, and streptolysins O and S affected lysosomes in both systems. Staphylococcal beta-toxin, leucocidin and enterotoxin, Shiga neurotoxin, Serratia endotoxin, diphtheria toxin, tetanus neurotoxin, C. botulinum type A toxin, and C. perfringens epsilon-toxin were not active in either system. Staphylococcal delta-toxin, C. histolyticum collagenase, crude C. perfringens beta-toxin, and crude anthrax toxin caused lysosomal damage in only one of the test systems. There is a substantial correlation between the hemolytic property of a toxin and its capacity to disrupt lysosomes, lending support to the concept that erythrocytes and lysosomes are bounded by similar membranes.

Topics: Acid Phosphatase; Animals; Antitoxins; Diphtheria Toxin; Endotoxins; Glucuronidase; Hemolysis; Leukocidins; Leukocytes; Liver; Lysosomes; Rabbits; Streptolysins; Tetanus Toxin; Toxins, Biological

Topics: Acid Phosphatase; Clinical Laboratory Techniques; Formaldehyde; Hemolysis; Humans; Laboratories; Phosphoric Monoester Hydrolases