acid-phosphatase and Hypoxia

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Creatine Kinase; Deoxyribonucleases; Dogs; Enzymes; Fructose-Bisphosphate Aldolase; Glutamate Dehydrogenase; Guinea Pigs; Humans; Hypoxia; Isocitrate Dehydrogenase; L-Lactate Dehydrogenase; Malate Dehydrogenase; Muscles; Ornithine Carbamoyltransferase; Physical Exertion; Pyruvate Kinase; Trehalase

Our purpose was to investigate the oxygen partial pressure changes on the osteometric and biochemical markers of bone tissue in rats. It was shown that breathing of altered gas mixture did not change the mass, general length, sagittal diameter and density thigh-bones in 12-month Wistar male-rats. The dosed normobaric hypoxia increased the activity of alkaline phosphatase and decreased the activity of tartrate-resistant acid phosphatase. At the same time normobaric hyperoxia with 40 and 90% oxygen conversely decreased the activity of alkaline phosphatase and increased the activity of tartrate-resistant acid phosphatase.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Bone Density; Bone Regeneration; Bones of Lower Extremity; Hypoxia; Isoenzymes; Male; Oxygen; Partial Pressure; Rats; Rats, Wistar; Tartrate-Resistant Acid Phosphatase

Mitochondria and lysosomes were evaluated by assessment of changes in activity of selected enzymes: lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), adenosinetriphosphatase (ATPase), acid phosphatase (AcPase) and beta-glucuronidase (BG) in rats under profound hypoxia induced by endotoxemic shock. The study was conducted on adult male Wistar rats. The animals formed the following four groups of 15 rats each: control animals (C);-rats receiving intraperitonally O(2)/O(3) (CO), rats receiving of Escherichia coli toxin (LPS) (CL); rats receiving LPS plus oxygen-ozone mixture (OL). Histoenzymatic examinations of liver, kidney, lungs, and heart muscle were performed. Lipopolysaccharide suppressed activities of all the enzymes except for LDH, the activity of which as high as a fourfold increase. The results demonstrated potent, stabilizing and regenerative effects of ozone therapy on body enzymatic processes in course of induced endotoxemic shock in rats, which might prove to be of clinical significance.

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Biomarkers; Glucuronidase; Hypoxia; Infusions, Parenteral; Kidney; L-Lactate Dehydrogenase; Lipopolysaccharides; Lung; Lysosomes; Male; Mitochondria; Myocardium; Oxidants, Photochemical; Oxygen; Ozone; Rats; Rats, Wistar; Shock, Septic; Succinate Dehydrogenase

Previously we showed that mitochondrial dysfunction induced by mitochondrial DNA depletion or treatment with electron transport chain inhibitors triggers a stress signaling involving activation of calcineurin and Ca2+-responsive factors. In this study we show that exposure of RAW 264.7 cells to hypoxia, causing increased reactive oxygen species (ROS) production and disruption of mitochondrial transmembrane potential, also induced a similar stress signaling. Hypoxia caused increased [Ca2+]c, activation of cytosolic calcineurin and induced expression of Ryanodine Receptor 2 (RyR2) gene. Prolonged hypoxia (5% O2 for 5-6 days) also induced the expression of calcitonin receptor at high levels, and those of cathepsin K, and tartarate-resistant alkaline phosphatase (TRAP) at low-moderate levels in macrophage cells. Addition of RANKL had an additive effect suggesting different mechanisms of activation. Consistent with this possibility, prolonged hypoxia induced the formation of TRAP-positive osteoclast-like cells suggesting the occurrence of an autocrine mechanism for osteoclastogenesis.

Topics: Acid Phosphatase; Animals; Calcineurin; Calcium; Cathepsin K; Cathepsins; Cell Differentiation; Cell Line; Cytosol; Gene Expression Regulation; Hypoxia; Isoenzymes; Macrophages; Membrane Potentials; Mice; Mitochondria; Osteoclasts; Signal Transduction; Tartrate-Resistant Acid Phosphatase

We studied the role of autochthonous microflora from body cavities in the development of tissue hypoxia and instability of cell membranes. In children with tuberculosis dysbiosis manifested in nonspecific quantitative changes in the intestinal microflora and the presence of coxsackievirus antigens in the urine. DNA-containing viruses with pronounced immunosuppressive activity (e.g., herpesvirus, measles virus, and rubella virus) were found in most children. Microbiological and virological changes were accompanied by the appearance of laboratory signs for tissue hypoxia, which included inhibition of Krebs cycle dehydrogenases and alpha-glycerophosphate pathway in blood lymphocytes. Regression analysis revealed a relationship between the content of extraintestinal coxsackieviruses and inactivation of alpha-glycerophosphate dehydrogenase, succinate dehydrogenase and ratio of facultatively anaerobic bacteria in microbiocenosis, and expression of acid phosphatase and total population of malonate-positive enterobacteria, staphylococci, yeasts, and enterococci.

Topics: Acid Phosphatase; Child; Child, Preschool; Enterobacteriaceae; Enterovirus; Glycerolphosphate Dehydrogenase; Humans; Hypoxia; Infant; Intestines; Lymphocytes; Tuberculosis; Urine

We studied the state of lysosomal apparatus and pro- and antioxidant activity in the liver of rats with different resistance to hypoxia during postischemic recovery. Under normal conditions the lysosomal apparatus did not differ in highly and low resistant animals. During ischemia and reperfusion the damage to hepatic lysosomal membranes in rats highly resistant to hypoxia was less pronounced than in low resistant animals. These differences also concerned labilization of lysosomes during exposure to damaging factors (hypotonia and Triton X-100). The rats highly resistant to hypoxia differed from low resistant animals by higher stability of lysosomal membranes, lower prooxidant activity (malonic dialdehyde content), and higher tissue concentration of alpha-tocopherol during reperfusion.

Topics: Acid Phosphatase; alpha-Tocopherol; Animals; beta-Galactosidase; Hypoxia; Intracellular Membranes; Ischemia; Liver; Lysosomes; Male; Malondialdehyde; Octoxynol; Oxidative Stress; Rats; Rats, Wistar; Reperfusion Injury; Ribonucleases; Time Factors

The Venus clam Chamelea gallina is fairly common along the western coasts of the Adriatic and is subjected to intense fishing. Since over the last 20 years extensive hypoxic and anoxic conditions have repeatedly damaged this natural resource, we decided to study the effects of anoxic stress on the functionality of clam haemocytes and the consequences on immune responses. Clams, exposed to air, close their valves and tissues become anoxic and metabolism processes switch to anaerobiosis. In these conditions, a significant decrease in the haematocrit value and in the percentage of acid phosphatase-positive haemocytes was observed, while the number of cells with beta-glucuronidase significantly increased after day 1. The above indices generally returned to control values when clams were re-immersed in seawater after 1 day of treatment. Clams exposed to air for 2 days and then re-immersed, attempted to recover in the subsequent 3 days. Animals had fully recovered on day 4. Three-day-exposed clams did not recover. Phagocytic and adhesion indices decreased significantly after the first day of air exposure. The change in frequency of three types of circulating cells (spreading, round, apoptotic) was also monitored.

Topics: Acid Phosphatase; Adaptation, Physiological; Air; Animals; Bivalvia; Cell Adhesion; Ecosystem; Glucuronidase; Hematocrit; Hemocytes; Hypoxia; Phagocytosis

It was studying the effect of fluorinecontain pinacidil analogs (PF-5 and PF-10), which are the K(+)-channel openers, on morphofunctional lysosomes state at lung and heart tissues. The investigation was made on white pubertal rat-males under acute (30 min) hypoxic hypoxia (7% O2 [symbol: see text] N2). The application of PF-5 and PF-10 under acute hypoxic hypoxia leads in lung and myocardium tissues to morphofunctional changes of lysosome system in investigated cells, which were connected with decreasing of enzyemia. It, partly, may be explain by increasing of connected enzyme forms synthesis, because such forms are the functional latent, so the output of enzymes in blood under unfavourable conditions increased.

Topics: Acid Phosphatase; Acute Disease; Animals; Cathepsin D; Disease Models, Animal; Heart; Hypoxia; Lung; Lysosomes; Male; Myocardium; Pinacidil; Potassium Channels; Rats; Rats, Wistar

We studied the activity of lysosomal enzymes (acid phosphatase and cathepsine D) and the status of lysosomal membranes of the liver, lung, heart and brain tissues of the male adult rats under acute hypoxia. We found that disturbances of lysosomal membranes permeability in these organs depend on the tissues hypoxia development, not yet on the genesis of hypoxic state. The lysosomal enzymes activation depends on the heaviness of the hypoxic influence.

Topics: Acid Phosphatase; Acute Disease; Animals; Brain; Cathepsin D; Disease Models, Animal; Heart; Hypoxia; Intracellular Membranes; Liver; Lung; Lysosomes; Male; Myocardium; Rats; Rats, Wistar

During metamorphosis, the salivary glands of the blow-fly undergo programmed cell death. Data is presented indicating that this programmed cell death does not in many respects emulate classical apoptosis. The cells are seen to vacuolate and swell rather than condense and shrink. There appears to be a transient enhancement in autophagy and an increase in acid phosphatase activity. This is followed by the characteristic appearance of ribosomal and extracisternal sources of the enzyme leading to autolysis. There appears to be no lysosomal leakage of acid phosphatase. As in apoptosis, the mitochondria persist until the cell fragments. The nucleus, however, does not show the distinct chromatin margination and blebbing that is typical of apoptosis. These changes are compared with necrotic changes induced by experimental anoxia. Overall the results show that a programmed cell death distinct from classical apoptosis is taking place.

Topics: Acid Phosphatase; Animals; Apoptosis; Diptera; Histocytochemistry; Hypoxia; Lysosomes; Metamorphosis, Biological; Microscopy, Electron; Microscopy, Electron, Scanning; Necrosis; Ribosomes; Salivary Glands; Vacuoles

Circadian variations of mouse liver, brain and heart lysosomal susceptibility to hypoxia were investigated. Lysosomal disruption during hypoxia was estimated on the basis of the following measurements: changes in percentage free activity of beta-galactosidase and acid phosphatase, tissue loss of both lysosomal enzymes and accumulation of serum beta-galactosidase. When exposure to hypoxia took place at the end of the rest phase or at the beginning of the active phase, it was accompanied by maximum increase of percent free activity. This, presumably represents a diffusion of enzymes from lysosomes due to altered membrane permeability. However, hypoxia when occurring during the second part of the active phase and first part of the rest phase resulted in tissues loss of lysosomal enzymes and accumulation of serum lysosomal enzymes. This is believed to represent the release of lysosomal enzymes in bulk from damaged or ruptured lysosomal membranes.

Topics: Acid Phosphatase; Activity Cycles; Animals; beta-Galactosidase; Brain Chemistry; Circadian Rhythm; Hypoxia; Liver; Lysosomes; Male; Mice; Myocardium

Topics: Acid Phosphatase; Adolescent; Adult; Arm; Bone Neoplasms; Child; Female; Humans; Hyperbaric Oxygenation; Hypoxia; Leg; Lymphocyte Activation; Male; Osteosarcoma; T-Lymphocytes; Tourniquets

Rabbit hearts perfused under hypoxic conditions underwent progressive subcellular damage, which becomes irreversible by one hour. During the first 20 minutes of perfusion, minor dilation of mitochondria and condensation of nuclear chromatin were the only salient features of cell injury. By 40 minutes moderate mitochondrial swelling was evident in hypoxic myocytes. Moreover, an increase in degenerating mitochondria and autophagic vacuoles was apparent. Reperfusion after either 20 or 40 minutes of hypoxia restored contractility, and injured myocytes underwent a cellular repair process that involved a dramatic increase in lysosomal autoplagy. One hour of hypoxia yielded irreversibly injured myocytes. Upon reoxygenation, some of these cells displayed typical changes of necrosis, but others apparently underwent an abortive repair process involving the formation of large, probably nonfunctional lysosomes. These observations suggest that lysosomal autophagy is important in the efforts at repair that cardiac cells initiate during and after hypoxia.

Topics: Acid Phosphatase; Animals; Autolysis; Coronary Disease; Disease Models, Animal; Hydrolases; Hypoxia; In Vitro Techniques; Lysosomes; Male; Mitochondria, Heart; Myocardium; Oxygen Consumption; Rabbits

Tissue of normal-term placentas, after normal pregnancy and spontaneous delivery, was incubated under normoxic and hypoxic conditions. Placental tissue samples were taken under sterile conditions, immediately after delivery, and incubated six hours in a medium to which six per cent or 26 per cent oxygen were supplied. After incubation, the tissue was homogenised, and the following enzymes were determined in the supernatant: aldolase, lactate-dehydrogenase, alkaline phosphatase, acid phosphatase, and glucose-6-dehydrogenase. - The activities of aldolase, glucose-6-dehydrogenase, and acid phosphatase increased and those of lactate-dehydrogenase and acid phosphatase decreased under conditions of oxygen deficit. Such changes in enzyme activity seem to suggest that in hypoxia anaerobic glycolysis is likely to increase, while maternal-foetal exchange drops, all accompanied by beginning compensatory proliferation of the trophoblast.

Topics: Acid Phosphatase; Alkaline Phosphatase; Female; Fructose-Bisphosphate Aldolase; Fructosediphosphates; Glucose; Glucose Dehydrogenases; Humans; Hypoxia; L-Lactate Dehydrogenase; Lactates; Organ Culture Techniques; Placenta; Pregnancy

Studies were undertaken to determine the effect of arachidonic acid, the precursor of bisenoic prostanoic acid derivatives, on the response of the isolated, perfused rabbit liver to hypoxia. Two and one half hours of severe hypoxia resulted in significant increases in hepatic vascular perfusion pressure, tissue wet weight, and the rates of cellular loss of lactic dehydrogenase, malic dehydrogenase, and acid phosphatase into the perfusing medium. Hypoxia also increased the rate of hepatic PGF2 alpha production by 25% after 2 1/2 hours (p less than 0.05, hypoxia vs sham). The addition of arachidonic acid (0.1 microgram/g/min for 150 minutes) to the perfusion medium of hypoxic livers significantly attenuated the changes in perfusion pressure, tissue wet weight, and loss of cellular enzymes. Arachidonic acid administration increased the rate of PGF2 alpha production by 100% (p less than 0.05, sham vs hypoxia + arachidonic acid) within 30 min after hypoxia and maintained this rate for the duration of the study. These results demonstrate that hypoxia mediated prostaglandin F2 alpha synthesis in the rabbit liver can occur in the absence of neural and blood borne components and that significant activation of the arachidonic acid cascade via the administration of exogenous arachidonic acid has a salutary effect on hepatic hemodynamics and cellular integrity during hypoxia.

Topics: Acid Phosphatase; Animals; Arachidonic Acids; Hypoxia; L-Lactate Dehydrogenase; Liver; Malate Dehydrogenase; Organ Size; Oxygen Consumption; Perfusion; Pressure; Prostaglandins F; Rabbits; Time Factors

The initial phase and the development of myocardial focal necroses were studied in 50 rats adapted successively to intermittent high altitude. The altitude hypoxia was produced in a low pressure chamber (7000 m, five days a week, four hours daily). First-minute myocardial changes detected by histochemical methods were found after 4 exposures at a level of 3000 m and distinct ones after 8 exposures at a level of 4500 m. Histologically, acute focal necroses were found after 11 exposures at a level of 6000 m. Hypoxia and stress are suggested to account for these myocardial focal changes. During further adaptation no further acute focal necroses were observed.

Topics: Acid Phosphatase; Altitude; Animals; Cardiomyopathies; Hypoxia; Male; Necrosis; Rats; Succinate Dehydrogenase

Laboratory animals were kept for 2, 8 and 16 hours in a pressure chamber, the air of which contained 8% O2 and 92% N2. Histochemical and ultrastructural examinations revealed the following duodenal alterations: 1. The alkaline phosphatase activity of the epithelium and glandular epithelium showed no alteration; the acid phosphatase activity was slightly increased in hypoxia. 2. The succinic dehydrogenase and cytochrome C oxidase activities of the glandular epithelium showed a marked decrease. 3. Two hours of hypoxia led to destruction of the microvillous epithelium. Prolonged hypoxia resulted in the destruction of the microvilli as well as of the cuticula. 4. Hypoxia of short duration had no damaging effect on glandular epithelial cells. After 8 to 16 hours of hypoxia, glandular secretion was reduced and the epithelial cells were evacuated. From the findings of the present investigation it is concluded that the decrease in the production of protective intestinal juice, due to the damaging effect of hypoxia on the epithelium and glandular epithelium as well as on the mitochondria, and the increase in the absorption of the intestinal content should be considered responsible of the additional damages to the intestinal epithelium.

Topics: Acid Phosphatase; Acute Disease; Alkaline Phosphatase; Animals; Duodenum; Electron Transport Complex IV; Female; Hypoxia; Male; Rabbits; Succinate Dehydrogenase; Time Factors

Topics: Acid Phosphatase; Altitude; Animals; beta-Aminoethyl Isothiourea; Galactosidases; Glucuronidase; Hypoxia; Lysosomes; Male; Radiation Injuries; Rats

Comparative histochemical investigations of the livers and kidneys of female Sprague-Dawley rats were made: 1. after intoxication with O-pinacolyl-methyl-phosphonylfluoride (Soman), O,O-diethyl-O-p-nitrophenylphosphate (Paraoxon, E 600); 2. after starvation of 24 to 36 h; 3. after hypoxia for 24 h. From the results it is concluded that the fatty degeneration of liver and kidney after PE.-intoxication is caused by intracellular hypoxia. No fatty degeneration of the organs was observed following deprivation of food for 36 h. A decreased level of cholin which might be caused by the intoxication with PE., and which could be the reason for the fatty degeneration was not found. This was indicated by the unaltered evidence of phosphatids in the intoxicated animals.

Topics: Acid Phosphatase; Alkaline Phosphatase; Animals; Cytochrome Reductases; Electron Transport Complex IV; Esterases; Fatty Liver; Female; Glucose-6-Phosphatase; Glucosephosphate Dehydrogenase; Glucuronidase; Hydroxybutyrate Dehydrogenase; Hypoxia; Isocitrate Dehydrogenase; Ketoglutarate Dehydrogenase Complex; Kidney; Lipase; Lipid Metabolism; Liver; Malate Dehydrogenase; Organophosphorus Compounds; Paraoxon; Pyruvate Dehydrogenase Complex; Rats; Soman; Starvation; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Dogs; Hypothermia, Induced; Hypoxia; L-Lactate Dehydrogenase; Myocardium; Subcellular Fractions

Topics: Acid Phosphatase; Adenosine Triphosphatases; Alkaline Phosphatase; Animals; Capillary Permeability; Cell Membrane; Cytoplasm; Dogs; Endoplasmic Reticulum; Extracorporeal Circulation; Glucose-6-Phosphatase; Glycogen; Hematocrit; Histocytochemistry; Humans; Hypoxia; Liver; Liver Circulation; Lysosomes; Mitochondria, Liver; Necrosis; Succinate Dehydrogenase

Topics: Acid Phosphatase; Animals; Cobalt; Erythropoiesis; Erythropoietin; Female; Glucuronidase; Histocytochemistry; Hypoxia; Iron; Kidney; Lysosomes; Male; Manganese; Membranes; Mice; Microscopy, Electron; Mitochondria; Nephrectomy; Nickel; Polycythemia; Rats

A biochemical assay of renal viability previously described for rabbits is validated in a canine model using anoxia, hypothermia, and hypothermic perfusion. The assay correlated well with the decree of anoxic injury and protective effect of hypothermia. It was found to be unable to document significant injury when pulsatile perfusion was added to the system and resulted in nonviable canine kidneys. Apparent vascular damage with interstitial hemorrhage occurred after the perfusion and was not predictable by the use of the assay system. The limitations of any assay for organ viability after complex preservation maneuvers is the result of a multiplicity of injurious factors surrounding the preservation or as a consequence of the preservation. No single assay system will be adequate for protection of organ viability during or after preservation as long as the types of injury are multiple. Is is suggested that great care be used in defining possible injurious factors associated with given preservation maneuver and that specific assays be utilized to document the effects of each of these factors. The more complex the preservation system employed; the more complex the assay system needed.

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Autopsy; Dogs; Female; Glucuronidase; Hypothermia, Induced; Hypoxia; Kidney; Kidney Transplantation; L-Lactate Dehydrogenase; Lactates; Male; Nephrectomy; Organ Preservation; Perfusion; Time Factors; Tissue Preservation

Topics: Acid Phosphatase; Animals; Bile; Blood; Carbon; Colloids; Endothelium; Fasting; Hemoglobins; Hydrogen-Ion Concentration; Hypoxia; In Vitro Techniques; Inclusion Bodies; Lactates; Liver; Liver Function Tests; Male; Microscopy, Electron; Osmolar Concentration; Perfusion; Potassium; Rats

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Disease Models, Animal; Hypoxia; Lysosomes; Male; Microelectrodes; Mitochondria, Liver; Muscles; Oxygen; Proteins; Rats; Shock, Hemorrhagic; Shock, Septic; Spectrophotometry

Topics: Acid Phosphatase; Alanine Transaminase; Animals; Aspartate Aminotransferases; Cell Membrane; Cell Membrane Permeability; Chlorpromazine; Cold Temperature; Computers; Dogs; Hypoxia; Ischemia; Isoproterenol; Liver; Membrane Potentials; Methylprednisolone; Microelectrodes; Oxygen; Perfusion; Potassium; Time Factors; Tissue Preservation; Tissue Survival; Tromethamine

Topics: Acid Phosphatase; Aorta; Child, Preschool; Cyanosis; Erythrocytes; Glucosephosphate Dehydrogenase; Heart Defects, Congenital; Humans; Hypoxia; Infant; Infant, Newborn; Pulmonary Artery; Tetralogy of Fallot; Transposition of Great Vessels

Topics: Acid Phosphatase; Adenosine Triphosphatases; Animals; Hypoxia; Liver; Lysosomes; Male; Microscopy, Electron; Mitochondria, Liver; Oxygen Consumption; Rats; Shock, Hemorrhagic; Shock, Septic; Time Factors

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Bloodletting; Cell Membrane Permeability; Dogs; Hemorrhage; Hypoxia; Male; Phosphoric Monoester Hydrolases; Prothrombin; Time Factors; Transaminases

1. Five-day-old anaesthetized rats subjected to slow, prolonged asphyxia (50-55 min) were either allowed to die or resuscitated when at the point of death. Activities of various cerebral acid hydrolases known to be associated with lysosomes were determined in these animals and in littermate controls. 2. Asphyxia to death resulted in a significant increase in the activities of acid phosphatase, cathepsin (pH5.0) and beta-glucuronidase in whole-brain homogenates. 3. The effect of asphyxia on beta-glucuronidase activity was not apparent when the assay was performed in the presence of Triton X-100 (0.1%, v/v). 4. In resuscitated animals whole-brain-homogenate beta-glucuronidase activity showed the greatest increase (31%) 15 min after recovery. After a 60 min recovery period differences between control and asphyxiated animals were no longer apparent. 5. In animals anoxiated to death activities of acid phosphatase and beta-N-acetylglucosaminidase in brain high-speed supernatants were significantly higher than in controls. Acid phosphatase activity was similarly increased in asphyxiated animals resuscitated for 5 or 60 min. 6. It is suggested that the response of the immature rat brain to asphyxia involves a disruption or increased fragility of lysosomal particles.

Topics: Acid Phosphatase; Animals; Brain; Cathepsins; Glucuronidase; Hexosaminidases; Hydrolases; Hypoxia; Lysosomes; Male; Postmortem Changes; Proteins; Rats; Resuscitation; Time Factors

Topics: Acid Phosphatase; Animals; Dogs; Glucuronidase; Hypoxia; Kidney; L-Lactate Dehydrogenase; Lactates; Leucyl Aminopeptidase; Perfusion; Pyruvates; Shock, Hemorrhagic; Temperature; Time Factors

Topics: Acid Phosphatase; Alanine Transaminase; Alkaline Phosphatase; Animals; Aspartate Aminotransferases; Cholinesterases; Diagnosis, Differential; Enzymes; Hypoxia; Kidney Diseases; L-Lactate Dehydrogenase; Leucyl Aminopeptidase; Malate Dehydrogenase; Male; Mercury Poisoning; Pyelonephritis; Rabbits

Topics: Acid Phosphatase; Alanine Transaminase; Animals; Haplorhini; Hypoxia; Liver; Liver Regeneration; Lysosomes; Macaca; Mitochondria, Liver; Portacaval Shunt, Surgical

Topics: Acid Phosphatase; Acidosis; Animals; Blood Volume; Capillary Permeability; Cardiac Output; Dogs; Embolism, Fat; Hemoglobins; Hypoxia; Isoenzymes; Lung; Lysosomes; Oils; Oleic Acids; Pulmonary Circulation; Pulmonary Embolism; Respiratory Dead Space; Shock, Hemorrhagic; Ventilation-Perfusion Ratio

Topics: Acid Phosphatase; Animals; Brain; Cerebral Cortex; Cerebrovascular Disorders; Disease Models, Animal; Glucuronidase; Glycogen; Hemiplegia; Hydrolases; Hypoxia; Hypoxia, Brain; Ischemic Attack, Transient; Lysosomes; Male; Mitochondria; Rats

Topics: Acid Phosphatase; Age Factors; Animals; Animals, Newborn; Humans; Hypoxia; Infant; Infant, Newborn; Lymphocytes

Topics: Acid Phosphatase; Animals; Glucosephosphate Dehydrogenase; Glucuronidase; Heart; Hematocrit; Hypoxia; Isocitrate Dehydrogenase; Isoenzymes; L-Lactate Dehydrogenase; Male; Myocardium; NADP; Nicotine; Rats

Topics: Acid Phosphatase; Antigen-Antibody Reactions; Glucosephosphate Dehydrogenase; Histocytochemistry; Humans; Hypoxia; Isocitrate Dehydrogenase; Kidney Glomerulus; Kidney Transplantation; Kidney Tubules; L-Lactate Dehydrogenase; Microscopy; Transplantation Immunology; Transplantation, Homologous

Topics: Acid Phosphatase; Adaptation, Physiological; Animals; Aortic Coarctation; Deoxyribonucleases; Disease Models, Animal; Heart; Heart Diseases; Hypoxia; Isoproterenol; Lysosomes; Male; Methods; Myocardium; Rats; Ribonucleases

Topics: Acid Phosphatase; Adaptation, Physiological; Altitude; Animals; Aortic Coarctation; Deoxyribonucleases; Heart Diseases; Hypoxia; Isoproterenol; Lysosomes; Male; Myocardium; Rats; Ribonucleases

Topics: Acid Phosphatase; Animals; Cytoplasm; Histocytochemistry; Hypoxia; Liver; Lysosomes; Male; Rats

Topics: Acid Phosphatase; Animals; Cholesterol; Coronary Vessels; Dogs; Electron Transport Complex IV; Hypoxia; Ischemia; Microscopy, Electron; Mitochondria; Myocardium; Oxygen Consumption; Phospholipids; Proteins; Triglycerides

Topics: Acid Phosphatase; Adrenal Glands; Adrenocorticotropic Hormone; Alkaline Phosphatase; Animals; Cats; Cattle; Female; Fetus; Guinea Pigs; Histocytochemistry; Horses; Humans; Hypoxia; Male; Mice; Rabbits; Rats; Sex Factors; Sheep; Species Specificity; Starvation

Topics: Acid Phosphatase; Animals; Dogs; Glucuronidase; Hemodynamics; Histocytochemistry; Hypoxia; Intestinal Mucosa; Liver; Lysosomes; Necrosis; Shock, Hemorrhagic

Topics: Acid Phosphatase; Animals; Chloroquine; Coloring Agents; Glucuronidase; Histocytochemistry; Hypoxia; Liver; Lysosomes; Male; Rats

Topics: Acid Phosphatase; Alanine Transaminase; Altitude; Animals; Aspartate Aminotransferases; Hypoxia; In Vitro Techniques; Liver; Lysosomes; Rats

Topics: Acid Phosphatase; Amylases; Glycine; Hypoxia; Ion Exchange Resins; Pancreas; Proteins; Rats; Research; Ultracentrifugation

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

Topics: Acid Phosphatase; Animals; Brain; Brain Diseases; Histocytochemistry; Hypoxia; Hypoxia-Ischemia, Brain; Hypoxia, Brain; Lysosomes; Phosphoric Monoester Hydrolases; Rats

Topics: 5'-Nucleotidase; Acid Phosphatase; Alkaline Phosphatase; Hypoxia; Infarction; Kidney; Kidney Diseases; Oxygen; Phosphoric Monoester Hydrolases; Protein Tyrosine Phosphatases