Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Acid phosphatase II (AP II) was isolated from the cell-free extract of Pichia guilliermondii Wickerham ATCC 9058 and partially purified. The enzyme is a non-specific phosphomonoesterase. It hydrolyzes p-nitrohenyl-phophate (NPP), beta-glycerophosphate, glucose-6-phosphate, guanosine-5'-monophosphate, adenosine-5'-monophosphate, cytidine-5'-monophosphate, uridine-5'-monophosphate, alpha-naphtylphosphate, FMN. The order of the substrates corresponds to the degree of their hydrolysis decrease. The Michaelis constant of the enzyme was 1.4-10-3 M for NPP as a substrate, pH optimum was 5.5 and temperature optimum-40C. AP II was strongly inhibited by MoO4-2, F-, inorganic phosphate, Cu2+ and Be2+. The activity of the enzyme in the yeast cells does not change noticeably during growth on media with low and high iron content.
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PMID:[Study of acid phosphatase II from Pichia guilliermondii yeasts]. 0 63

The activity of acid phosphatase in the testicular parenchyma of cattle was found to be higher than that in the endometrium. The acid phosphatase of either tissue broke up p-nitrophenylphosphate at a rate twice as high as that reached for di-sodium phenylphosphate. Hydrolysis of phenolphthalein diphosphate was slower and that of beta-glycerophosphate very slow. Two optimum pH values and two isozymes were recordable from acid phosphatase in testicular supernatant and three optimum pH values as well as three isozymes from that in endometrial supernatant. Even concentrations pf 0.2 mM of copper and mercury ions were strongly inhibiting the acid phosphatase, whereas lead and cadmium ions proved less effective. The activity of acid phosphatase from testes dropped by 24 per cent and that from the endometrium by 16 per cent over eight weeks of storage at -20 degrees C. The average activity of alkaline phosphatase in the endometrium was much higher than that in testicular parenchyma. Alkaline phosphatase from testes exhibited the shortest break-up time for p-nitrophenylphosphate, whereas disodium-phenylphosphate was broken up at the highest rate by endometrial alkaline phosphatase. Two isozymes of alkaline phosphatase were recordable each from the testes and endometrium.
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PMID:[Properties and isozymes of acid and alkaline phosphatase in cattle testes and endometrium]. 2 59

To see whether urine enzyme activities could be used as an index in evaluating the disease status of leukemia patients, we examined the activities of four enzymes: arylsulfatases A(AS-A) and B(AS-B), alkaline phosphatase (AP), and lactate dehydrogenase (LDH). AP and LDH showed no consistent patterns. The activities of AS-A and AS-B correlated well with the patient's clinical status, increasing during progression of disease and decreasing toward normal activities during responses to therapy, as judged from bone marrow cellularity and differential. Among 23 untreated patients with a histologic diagnosis of acute leukemia we found increased activities of the urine enzymes in these proportions: AS-A in 23 patients (100%), AS-B in 22 (95.7%), AP in 7 (30.4%), and LDH in 10 (43.5%). Five patients in remission from acute leukemia had normal activities for all four enzymes. In one patient in remission for more than one year, a rise in urinary arylsulfatase activity preceded observable bone marrow relapse by 4 months. Unlike that of serum of urine lysozyme and serum copper, the determination of urine arylsulfatase activities appears to be a consistent, useful indicator of response to antileukemic therapy. In contrast to the determination of polyamines, the quantitation of arylsulfatase activity is achieved with greater ease and with instrumentation available in most clinical laboratories.
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PMID:A noninvasive technique for monitoring response to chemotherapy in human acute leukemia. 3

5'-Nucleotidase, assayed as 5'-AMPase, has been extensively characterized and established as a stable, quantitative plasma membrane marker in HeLa S3 cells. The membrane 5'-AMPase has a Km of 7.0 microM. Relative affinities of the other 5'-mononucleotides for the enzyme are 5'-GMP > 5'-TMP > 5'-UMP > 5'-CMP. There are activity optima at pH7 and 10; the latter is Mg(2+)-dependent. The membrane preparations have a small amount of acid phosphatase activity that is distinct from 5'-AMPase activity but no alkaline phosphatase. AOPCP, ADP, and ATP are strongly inhibitory. Mg2+, Ca2+, or Co2+ additions do not affect the pH 7.0 activity; Mn2+ activates slightly, whereas Zn2+, Cu2+, and Ni2+ are inhibitory. EDTA slowly inactivates, but removal of the EDTA without the addition of divalent cations restores activity. The inactivation is also substantially reversed by Co2+ or Mn2+, but reactivability by divalent cations decreases with time in EDTA. ConA strongly inhibits, and alpha-methyl-D-mannoside or glucose (the latter much less efficiently) relieves the inhibition, indicating that the 5'-AMPase is a glycoprotein. Histidine is also inhibitory. Ouabain, phloretin, cytochalasin B, cysteine, phenyl-alanine, MalNEt, and IAA are without effect. 5'-AMPase activity codistributes with pulse-bound [3H]ouabain when either of two cell fractionation procedures are used. The 5'-AMPase activity per cell is constant at different cell densities in exponentially growing cells, and activity per unit cell volume remains constant throughout the cell cycle. These properties, together with its absence in other organelles, its stability to storage, its insensitivity to certain experimental manipulations, and its general insensitivity to inhibitors of specific transport systems, make 5'-AMPase a useful quantitative marker in studies on the regulation of HeLa membrane transport systems. Key Words: HeLa, 5'-nucleotidase, plasma membrane marker, non-specific phosphatases, divalent ions, ConA, AOPCP, cell cycle, mitochondria, transport inhibitors.
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PMID:Characterization of HeLa 5'-nucleotidase: a stable plasma membrane marker. 4 80

Clinical, biochemical and immunological variables were analyzed in 30 patients with orcein-negative (ON) chronic active hepatitis (CAH), 4 patients with ON primary biliary cirrhosis (PBC), 8 patients with orcein-positive (OP; intracellular copper-binding protein seen histologically in liver biopsy specimens) CAH and 15 patients with OP-PBC. A marked elevation of serum bile acids, alkaline phosphatase, leusine aminopeptidase, gammaglutamyl transpeptidase and cholesterol concentrations, and highly pathological BSP Tm values were characteristic for OP-cases. In addition the faecal fat level was increased and bile acids decreased in OP-cases. Serum levels of IgG or IgM and the occurrence of smooth muscle, mitochondrial or glomerular antibodies were identical in ON- and OP-CAH as well as also in ON- and OP-PBC. 49 patients were treated with a combination of prednisone and azathioprine from 4 to 72 months (mean 22). 26 patients with ON-CAH responded biochemically and morphologically to the treatment. No treatment failures were found in ON-CAH. In contrast treatment failure was confirmed in every treated OP-PBC or OP-CAH. The results suggest that orcein-positivity indicates a poor response to prednisone-azathioprine treatment of CAH.
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PMID:Clinical correlations and significance of orceinpositivity in chronic active hepatitis and primary biliary cirrhosis. 6 65

A significant positive correlation between serum zinc and serum alkaline phosphatase levels was demonstrated in four patients suffering from acrodermatitis enterophathica for which they received oral zinc sulphate therapy. In one of the male patients a significant inverse relation between serum zinc and serum copper was found.
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PMID:Serum alkaline phosphatase activity in acrodermatitis enteropathica: an index of the serum zinc level. 8 82

The following blood indices were determined in the blood of 34 pregnant sows of the Large White breed under standard feeding conditions: haemoglobin, haematocrit, leucocytes, and--in the blood serum, --total protein, glucose, urea, bilirubin, cholesterol, enzyme activity (AP, GOT, GPT, GGTP) and mineral concentrations (Ca, P--inorg., Mg, Na, K, Fe, Cu, Zn, Mn). The blood was sampled in the first and third pregnancy at an average live weight of 165.12 and 197.36 kg, at an average age of 318 and 630 days and at an about the same average length of pregnancy in the time of both samplings (59 days). In younger, still growing gilts (first pregnancy) a significantly (P less than 0.05) lower content of total protein, magnesium, iron and copper was revealed, as compared with adult sows. The content of glucose, calcium, potassium and manganese in the blood serum of the gilts was significantly (P less than 0.05) higher than in sows in their third pregnancy. The adult sows showed a significantly (P less than 0.05) lowered activity of alkaline phosphatase and gamma-glutamyl transpeptidase, as distinct from gilts.
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PMID:[The effect of pregnancy order on various biochemical and hematological values in sows]. 10 42

Whole blood samples from 40 male and 40 female individuals were analyzed for zinc, copper, selenium and iron, and in part also for cadmium and lead. Correlations were established between the element contents and the activities of blood enzymes (carbo-anhydrase, leucine aminopeptidase, lactate dehydrogenase, alkaline phosphatase, glutathione peroxidase). The zinc-copper ratio exerted no effect on the zinc-dependent enzymes. There was a correlation between the glutathione peroxidase activity and the selenium content in whole blood (r greater than 0.73). A cluster analysis was performed. In women, the authors stated a significant effect of oral contraceptives especially on the zinc and copper balance. It was evidenced that detectable (more marked) changes in the mineral equilibrium are not produced in all cases by the contraceptives. Nevertheless, changes in the mineral equilibrium are likely to occur in 25% of all women. In the present study further changes (for example in enzymes) were observed in 50% of all women. The results obtained from the male individuals were indicative of certain relationships between the zinc-copper ratio and the content of total lipids or lipid fractions in human blood.
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PMID:[Effect of the trace element supply on element dependent enzymes in man]. 11 Nov 26

Normal values for a number of blood components of grivet monkeys are reported. Haematological data and values for glucose, cholesterol and urea are similar to those of rhesus monkeys. Activities of alkaline phosphatase (1526 U/l), glutamine oxaloacetate transaminase (30.9 U/l), glutamine pyruvate transaminase (13.7 U/l), lactate dehydrogenase (629 U/l), alpha-hydroxybutyrate dehydrogenase (175 U/l), creatine phosphokinase (227 U/l), gamma-glutamyl transpeptidase (38.7 U/l) and sorbitol dehydrogenase (14.2 U/l), and levels of lysozyme (178 mg/dl), zinc (162 microgram/dl), copper (81.3 microgram/dl) and iron (296.5 microgram/dl) have not previously been reported for this animal. Values for serum amino acids, proteins, electrolytes, triglycerides and creatinine are compared with those of other primates.
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PMID:Normal values for some whole blood and serum components of grivet monkeys (Cercopithecus aethiops). 11 24

The conditions necessary for the secretion of phospholipase C (phosphatidylcholine cholinephosphohydrolase) by Pseudomonas aeruginosa were studied. Enzyme secretion by washed cell suspensions required a carbon source and ammonium, potassium, and calcium ions. The calcium requirement could be substituted by magnesium and strontium but not by copper, manganese, cobalt, or zinc. During growth in liquid medium, cells secreted phospholipase C during late logarithmic and early stationary phases. Secretion was repressed by the addition of inorganic phosphate but not by organic phosphates, glucose, or sodium succinate. Studies with tetracycline indicated that de novo protein synthesis was necessary for the secretion of phospholipase C and that the exoenzyme was not released from a preformed periplasmic pool. Similarly, extraction of actively secreting cells with 0.2 M MgCl2 at pH 8.4 solubilized large quantities of the periplasmic enzyme alkaline phosphatase but insignificant amounts of phospholipase C. Bacteria continued to secrete enzyme for nearly 45 min after the addition of inorganic phosphate or rifampin.
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PMID:Secretion of phospholipase C by Pseudomonas aeruginosa. 11 87


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