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)

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

Porcine rotaviral infectivity for continuous porcine kidney (PK-15) cells was enhanced by incorporation of pancreatic endopeptidases into the cell culture maintenance medium. Marked enhancement of infectivity was induced by trypsin, whereas elestase and alpha-chymotrypsin enhanced infectivity to a lesser extent. Bacterial protease also induced some enhancement of porcine rotaviral infectivity. A synergistic enhancement of porcine rotaviral infectivity was noticed with trypsin and alpha-chymotrypsin combined. Porcine rotaviral infectivity was not affected by incorporation of alpha-amylase, alkaline phosphatase, beta-galactosidase, carboxypeptidase-A, deoxyribonuclease, enterokinase, lipase, or ribonuclease into the maintenance medium.
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PMID:Porcine rotaviral infection of cell culture: effects of certain enzymes. 624 64

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

Although zinc in traces is essential for the growth and well being of the animal, however a long-term treatment has been found equally toxic to the liver and kidney. Present report describes its effects on few key enzymes viz. alkaline phosphatase, acid phosphatase, 5-nucleotidase, lipase, glucose-6-phosphatase, and cholinesterase in the liver of rat, Rattus rattus albino. Histochemical observations have provided visual evidences on Zn-induced dysenzymia. The results have further been interpreted in terms of its effects on cellular organelle, levels of enzyme protein and microenvironment of the hepatic parenchyma.
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PMID:A note on dysenzymia in the liver of rats fed on zinc, an essential metal. 629 52

Some hydrolases are localized cytochemically in the pollen and pollen tubes of Amaryllis vittata Ait. The function of different enzymes is discussed in relation to pollen tubes morphogenesis. Activity of most of the enzymes was confined to colpus region, pollen wall and general cytoplasm of pollen and pollen tube. The activity of hydrolytic enzymes like acid monophosphoesterase and lipase and was nil in the exine of both germinated and ungerminated pollen, whereas intense reaction for esterase was observed in exine. Enzyme activity increased after germination which suggest the hydrolysis of stored metabolites and synthesis of proteins and other metabolites for the active growth of pollen tube. Intense reaction for enzymes like alkaline phosphomonoesterase, ATP-ase, 5-nucleotidase etc. at the tip region of pollen tube suggest their role in physiological processes associated with exchange of materials through intercellular transport during tube wall polysaccharide biogenesis.
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PMID:Cytochemical localization of some hydrolases in the pollen and pollen tubes of Amaryllis vittata Ait. 629 81

An attempt has been made to observe the effects of chromium on a few enzymes, viz. alkaline phosphatase, acid phosphatase, glucose-6-phosphatase and lipase, in the kidney of the rat (Rattus rattus albino) by means of histochemical and biochemical criteria. Administered as potassium chromate in the diet, it was found to inhibit the activity of these renal enzymes; moreover, characteristic differences were observed in their anatomic localization. The possible effects of chromium on the level of enzyme protein and the state of the cellular organelles, together with modifications of biochemical processes such as phosphorylation, adenylation and oxidative phosphorylation, are discussed.
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PMID:Enzymological effects of hexavalent chromium in the rat kidney. 632 79

We isolated 15 mutants of Pseudomonas aeruginosa PAO which were defective in the formation of certain extracellular proteins, such as elastase, staphylolytic enzyme, and lipase ( Xcp mutants). The mutations were mapped on the chromosome by conjugation and transduction. The locations were xcp -1 near 0', with the gene order cys-59- xcp -1- proB , and loci xcp -2, xcp -3, and xcp -31 at 35', with the gene order trpC , D- xcp -3/ xcp -31- xcp -2- argC . Loci xcp -4 and xcp -41 through xcp -44 were cotransducible with proA at 40'; loci xcp -5, xcp -51, xcp -52, and xcp53 were located at 55', with the gene order leu-10- trpF -met-9010- xcp -53- xcp -5/ xcp -51/ xcp+ ++-52, and xcp -6 was located at 65' to 70', between catA and mtu-9002. Nine mutations ( xcp -2, xcp -3, xcp -31, xcp -4, and xcp -41 through xcp -45) caused decreased production of extracellular enzymes. Six strains with mutations xcp -1, xcp -5, xcp -51, xcp -52, xcp -53, and xcp -6 produced cell-bound exoproteins and had defective release mechanisms. The regulation of production of alkaline phosphatase and phospholipase C is different from other exoproteins , such as elastase, but they all seem to share a common release mechanism. Alkaline protease had separate mechanisms for regulation and release, since this protease was found in culture supernatants of all but one of the mutants, and none of the strains had cell-bound enzyme.
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PMID:Genetic mapping and characterization of Pseudomonas aeruginosa mutants defective in the formation of extracellular proteins. 642 94

Twelve whole mite extracts (WME) from seven sources were examined for their content of the allergen Dpt 12, protein content, and the inhibitory capacity in RAST by use of paper discs coupled with either WME or Dpt 12. Linear regression analysis demonstrated that the concentration of Dpt 12 determined either by single radial immunodiffusion or by RAST inhibition did not correlate with either the RAST-inhibition titer with use of discs coupled with WME or with protein content, suggesting that Dpt 12 content does not reflect the overall potency of WMEs. However, statistically significant correlations were obtained between Dpt 12 content and whole mite-RAST inhibition titers if extracts from the same manufacturer were examined or if data obtained from extracts containing large Dpt 12 to protein concentrations (greater than 25%) were excluded from the analysis. In contrast, statistically significant correlations between protein concentration and WME-RAST inhibition titers (p = 0.00037) and between Dpt 12 content and Dpt 12 RAST-inhibition titers (p = 0.00001) were found. Thermal stability studies demonstrated that Dpt 12 per se and WMEs were stable at 4 degrees C for up to 3 mo. Storage at 23 degrees C for 3 mo, however, resulted in partial loss of both Dpt 12 and whole-mite activity. Substantial losses occurred at 36 degrees C for both 1-month and 3-month incubation periods. Esterase, esterase lipase, and alkaline phosphatase were found in three WMEs studied. Dpt 12 was biochemically unrelated to these enzymes.
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PMID:Quantitation and thermal stability of the mite allergen DPT 12 in whole mite extracts. 643 11

A pancreas-specific antigen was identified by immunologic techniques and purified from saline extract of human pancreas. The purified pancreas-specific antigen was shown to be homogeneous by polyacrylamide gel electrophoresis under both denaturing and non-denaturing conditions. It had a molecular weight of 44000 as estimated by gel filtration or sodium dodecyl sulfate-gel electrophoresis, and a sedimentation coefficient of 3.4 S as analyzed by sucrose gradient centrifugation. Pancreas-specific antigen possessed an isoelectric point of 4.9 and migrated to alpha-beta region upon immunoelectrophoresis. By colorimetric assay procedures, pancreas-specific antigen exhibited no enzyme activity, such as amylase, protease, esterase, lipase, acid phosphatase, alkaline phosphatase peroxidase, deoxyribonuclease or ribonuclease. Immunoreactivity of pancreas-specific antigen was sensitive to proteolytic enzymes, perchloric acid and high temperature (70 degrees C, 10 min); but insensitive to neuraminidase or beta-glucosidase. Immunohistochemical staining revealed that pancreas-specific antigen was located in acinar cells of human pancreas. In addition, a higher concentration of pancreas-specific antigen was detected in pancreatic juice than in the saline extract of pancreas. This newly identified pancreas-specific antigen, therefore, may be a useful marker protein in physiological studies of pancreas and pancreatic secretion.
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PMID:Purification and characterization of a human pancreas-specific antigen. 678 69

Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase, alpha-galactosidase, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase, trypsin, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
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PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46


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