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)

Natural populations of Glossina morsitans submorsitans Newstead, Glossina palpalis gambiensis Vanderplank and Glossina tachinoides Westwood occurring within 150 km of Bobo-Dioulasso, Upper Volta were examined using polyacrylamide gel electrophoresis. No variation was found in the banding pattern for arginine phosphokinase (EC 2.7.3.3). G. p. gambiensis and G. tachinoides had three alleles for each of the thoracic enzymes octanol dehydrogenase (EC 1.1.1.73), malic dehydrogenase (EC 1.1.1.37) and alpha-glycerophosphate dehydrogenase (EC 1.1.1.8) and for midgut alkaline phosphatase (EC 3.1.3.1). The same situation was found with G. m. submorsitans except that only two alleles for alpha-glycerophosphate dehydrogenase and one for alkaline phosphatase were found. In each species, and for each of the enzymes, one allele was present at a frequency of 95% or greater. There was little or no variation between populations. Two laboratory colonies of G. p. gambiensis had less genetic variation than wild populations.
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PMID:Genetic polymorphism in three species of tsetse flies (Diptera: Glossinidae) in Upper Volta. 611 54

Human lymphocytes were isolated from defibrinated blood by Ficoll-Hypaque centrifugation with erythrocyte hypotonic lysis. Homogenates of mixed lymphocytes were subjected to analytical subcellular fractionation by sucrose gradient centrifugation in a Beaufay automatic zonal rotor. The principal organelles were characterized by their marker enzymes: cytosol (lactate dehydrogenase), plasma membrane (5'-nucleotidase), endoplasmic reticulum (neutral alpha-glucosidase), mitochondria (malate dehydrogenase), lysosomes (N-acetyl-beta-glucosaminidase), peroxisomes (catalase). gamma-Glutamyl transferase was exclusively localized to the plasma membrane. Leucine amino-peptidase, especially when assayed in the presence of Co2+, was also partially localized to the plasma membrane. Experiments with diazotized sulphanilic acid, a non-permeant enzyme inhibitor, showed that these plasma membrane enzymes are present on the cell surface. No detectable alkaline phosphatase was found in the lymphocytes. Acid phosphatase and beta-glucuronidase were localized to lysosomes and there was some evidence for lysosomal heterogeneity. Leucine amino peptidase, optimal at pH 8.0, showed a partial localization to intracellular vesicles, possibly lysosomes, especially when assayed in the presence of EDTA. These studies provide a technique for determining the intracellular distribution of hitherto unassigned lymphocyte constituents and serve as a basis for investigating the cell pathology of lymphocytic disorders.
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PMID:Enzyme analysis and subcellular fractionation of human peripheral blood lymphocytes with special reference to the localization of putative plasma membrane enzymes. 614 55

Activities of 12 enzymes (amylase, lipase, cholinesterase, nonspecific carboxyl esterase, lactate dehydrogenase (LDH), alkaline phosphatase, glutamate-oxalacetate transaminase (GOT), glutamate-pyruvate transaminase (GPT), gamma-glutamyl transferase (gamma-GT), leucine aminopeptidase (LAP), malate dehydrogenase (MDH) and peroxidase) were determined in the perienteric fluid and homogenate of Ascaris suum. With the exception of amylase, all activities were higher in the homogenate than in the perienteric fluid. The enzyme activities in the perienteric fluid were then compared with those in the human serum. Comparable activities were demonstrated for LDH, LAP, lipase and alkaline phosphatase, markedly higher activities in perienteric fluid were demonstrated for MDH, GOT, GPT and amylase, and much lower for cholinesterase. No gamma-GT activity was detected in the perienteric fluid.
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PMID:Activities of some enzymes in the perienteric fluid of Ascaris suum. 619 63

The effect of sodium dodecyl sulfate on the activity of highly purified or crystalline enzymes has been studied. The enzymes were: lactate dehydrogenase (LDH), malate dehydrogenase (MDH). isocitrate dehydrogenase (ICDH), glucose-6-phosphate dehydrogenase (G6P-DH), lipase, alkaline phosphatase. Sodium dodecyl sulfate, always under the critical micellar concentration, shows a selective inhibitory effect. A kinetic analysis of the inhibitory action on LDH, MDH, ICDH and G6P-DH was also carried out.
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PMID:[Sodium dodecyl sulfate, concurrent inhibitor of several dehydrogenases]. 621 65

Rabbit morulae were grown for 24 h in Ham's F12 medium supplemented with BSA. CI-628 citrate (1.5 micrograms/ml), a specific oestrogen antagonist, significantly inhibited the transformation of morulae to blastocysts. This inhibition was reversed with oestradiol-17 beta (1 micrograms/ml) but not oestradiol-17 alpha (1 micrograms/ml) added to the culture medium. The specific activities of phosphofructokinase, lactic dehydrogenase, malate dehydrogenase and alkaline phosphatase in blastocysts grown in vitro for 24 h in medium TC 199 + BSA showed significant elevation with blastocyst growth and expansion, while that of acid phosphatase revealed no change, and leucine aminopeptidase activity declined significantly. These changes were markedly inhibited by CI-628 citrate (2 micrograms/ml) and were reversed by oestradiol-17 beta (0.4 micrograms/ml) but not by oestradiol-17 alpha (0.4 micrograms/ml). Our findings suggest a role of oestrogen present in the rabbit morula and blastocyst in the triggering of embryonic differentiation and metabolic functions.
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PMID:Role of embryonic oestrogen in rabbit blastocyst development and metabolism. 623 Apr 43

As Paramecium caudatum passes through the lag, log and stationary phases of the culture cycle, cellular protein content, polar (PL) and neutral (NL) lipid contents, marker enzyme activities, rate of digestive vacuole formation and cellular viability undergo characteristic changes. Maximal protein content (60 ng/cell) and enzyme activities ranging from 7 nmoles for catalase to 0.2 pmoles/cell/min for alkaline phosphatase were observed between days 2 and 4. This active metabolism paralleled the fine structure of 1 to 3 day-old cells which contained extensive foci of rough endoplasmic reticulum (RER) partially bordered by Golgi stacks and the rapid depletion of those lipid fields accumulated during day 1. Decrease in protein content and enzyme activities in late log phase indicated a slowing of cellular synthesis. The lipids in the medium were largely depleted and accounted for the low lipid uptake of 14 ng/cell on day 5 as compared with 615 ng/cell on day 1. Yet a vast amount of protein lysate was still available in the culture medium. During stationary phase, catalase activity remained constant, but activities of alkaline and acid phosphatases and 5'nucleotidase declined gradually to low levels, while those of Ca2+-ATPase and malate dehydrogenase declined precipitously. Only 25% of the maximal activities of the latter two enzymes remained by the end of stationary phase. A ten-fold increase in the cellular PL and NL content was already observed 24 h postinoculation. This accumulation was used for subsequent growth and cell divisions; PL declined exponentially and NL less steeply between days 1 and 6. PL remained level (5 ng/cell) throughout stationary phase while NL declined further to 1 ng/cell by day 11. The rate of digestive vacuole formation was constant (6.3 +/- 0.5 DV/5 min pulse) during the entire log phase, then declined from 4.4 on day 6 to 0.22 on day 11. When early to mid-stationary-phase cells were subcultured, some lag in growth was seen; a definite lag was observed when inoculating with late-stationary-phase cells. When early-death-phase cells were given fresh nutrients, many died; the surviving ones became fully rejuvenated after 48 h. The biochemical and physiological data from this study are correlated with the morphological study of the companion paper.
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PMID:Axenic Paramecium caudatum. III. Biochemical and physiological changes with culture age. 626 57

The effect of 1-butanesulfonic acid sodium salt and sodium dodecyl sulfate on the activity of highly purified and crystalline enzymes with marked differences in structure and function has been studied. The enzymes were: alcohol dehydrogenase; lactate dehydrogenase; malate dehydrogenase; isocitrate dehydrogenase; glucose-6-phosphate dehydrogenase; lipase; alkaline phosphatase. While 1-butanesulfonic acid sodium salt, at the studied concentrations, resulted generally inactive, sodium dedecyl sulfate showed a selective inhibitory effect, always under the critical micellar concentration. A kinetic analysis of the inhibitory action was also carried out.
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PMID:Specific interaction among some enzymes and sodium dodecyl sulfate. 629 Aug 15

The activity of endocellular enzymes (alkaline phosphatase, protease, glucose dehydrogenase, aldolase, malate dehydrogenase, NADH dehydrogenase, NADH oxidase) was studied in isolated prospores and sporangia as well as in vegetative cells of Bacillus thuringiensis strains, one of which produced crystals and one did not. The activity of malate dehydrogenase and NADH dehydrogenase was high in prospores of the both strains at the fifth and sixth stages of spore formation. The strain which did not produce crystals differed from the parent strain by a higher aldolase activity at all of the growth stages and by an abrupt increase in the activity of hydrolytic enzymes in sporangia (in the cytoplasm of the parent cells).
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PMID:[Activity of intracellular enzymes in Bacillus thuringiensis prospores and sporangia]. 634 86

A study has been carried out in order to explain the enzyme-palmitoleate interaction. The highly purified and crystalline enzymes representative of fundamental metabolic pathways were: alcohol dehydrogenase (ADH), lactate dehydrogenase (LDH), malate dehydrogenase (MDH), isocitrate dehydrogenase (ICDH), glucose-6-phosphate dehydrogenase (G6P-DH), alkaline phosphatase. The enzyme-palmitoleate interaction was studied as a phenomenon time-independent (inhibition) and time-dependent (inactivation). Palmitoleate inhibited remarkably LDH, MDH, ICDH and G6P-DH. A kinetic analysis of the inhibitory action of palmitoleate on LDH and MDH was also carried out. Inactivation studies have shown that ADH and alkaline phosphatase are not sensitive to palmitoleate action, unlike the other enzymes. A comparison was made between the action of palmitoleate and that of a synthetic anionic detergent, sodium dodecyl sulfate (SDS).
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PMID:The palmitoleate: a natural selective denaturant of enzymes. 635 72

A naturally occurring enteropathy was identified in Irish setter dogs and wheat-sensitivity was demonstrated in a litter bred from two of the affected animals. The morphological and biochemical features of this enteropathy are described and compared to coeliac disease in man. Affected animals comprised 10 dogs that presented with poor weight gain or weight loss, with or without diarrhoea. Exocrine pancreatic function was normal and culture of duodenal juice demonstrated no marked bacterial overgrowth. Serum vitamin B12 concentrations were unaltered, but in some cases low serum and erythrocyte folate concentrations and reduced xylose absorption provided indirect evidence for proximal small intestinal disease. Examination of peroral jejunal biopsies revealed patchy morphological changes within individual animals, comprising predominantly partial, but in one case subtotal, villous atrophy. Brush border enzymes were selectively altered: the specific activities of alkaline phosphatase, leucyl-2-naphthylamidase and of zinc-resistant alpha-glucosidase were reduced by approximately 40 per cent, while activities of maltase, sucrase, lactase and gamma-glutamyl transferase were unaltered. Activity of a lysosomal enzyme was increased and there was evidence for enhanced lysosomal fragility. The activity of malate dehydrogenase, with a dual mitochondrial and cytoplasmic localisation, was decreased but there were no changes in the activities of marker enzymes for basal-lateral membranes, endoplasmic reticulum or peroxisomes. These findings, particularly the specific biochemical abnormalities, were comparable to those in partially treated coeliac disease in man; however, a specific role for wheat in the pathogenesis of the disease has yet to be defined.
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PMID:Morphological and biochemical studies of a naturally occurring enteropathy in the Irish setter dog: a comparison with coeliac disease in man. 652 28


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