Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Application of extracorporeal shock wave lithotripsy to gallbladder stones was studied in 37 adult female swine. Twenty-two sows underwent cholecystostomy with implantation of human gallstones. In 20 animals, after a 10-day recovery period, extracorporeal shock wave lithotripsy, 2000 shocks (an amount determined in preliminary water bath studies to be effective), was performed. In 10 of these implanted swine, frequent focal point refocusing and biplanar ultrasonography were employed. Two animals served as operative controls. Fifteen other animals without gallstone implantation were studied for adverse effects of extracorporeal shock wave lithotripsy on tissue. These animals (unimplanted) received 5000 shocks; 7 animals were killed 1 to 4 days after treatment and the others were killed after 4 weeks. Biochemical tests (total bilirubin, alkaline phosphatase, lipase, amylase, alanine aminotransferase, and lactate dehydrogenase determinations) were performed on all animals at entry and every second or third day until they were killed. Successful fragmentation, defined as all residual gallstone fragments being less than or equal to 4 mm in greatest dimension, was achieved in 14 of 20 animals overall, but in 10 of 10 animals in which focal point refocusing had been used. Slight perivascular hemorrhage and minimal coagulation necrosis were seen histologically only in the liver parenchyma adjacent to the gallbladder bed. The remainder of the liver was grossly and histologically normal. No injuries to the colon, duodenum, common bile duct, or pancreas were observed. No alterations suggesting injury or altered function occurred in any of the biochemical tests.
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PMID:Biliary lithotripsy. Determination of stone fragmentation success and potential tissue injury in swine. 275 4

Since they are found to be increased in lesions of acute necrotic ulcerative gingivitis or marginal periodontitis, agents for these diseases. In the present study, 38 pure cultured strains were obtained as a result of isolation and culture of samples collected from lesions of marginal periodontitis (periodontal pokets), and the biological and biochemical characteristics of these strains were investigated. 1) Light microscopy (including dark-field microscopy) and transmission electron microscopy (negative staining) were used for observation of the morphology and cellular structure of the strains. The cells had a spiral shape, and showed active movement. Based on the above findings the cultured strains were all confirmed to be spirochetes of small to medium size, being 0.08-0.24 micron in width. 2) Growth and motility of the strains were investigated on various types of culture medium. Intense growth and movement were noted in strains cultured in bovine liver exudate medium containing horse serum (pH 7.2) at 37 degrees C under anaerobic conditions produced by the evacuation-replacement method (95% N2, 5% CO2) for 3-7 days after inoculation. 3) Thirty-five strains were positive for indole production and decomposition of urea, mucin, hippuric acid and esculin. Production of hydrogen sulfied was observed in 31 strains. In decomposition tests for 17 carbohydrates, 17 strains were positive for galactose and 14 strains were positive for glucose, while 11 strains were positive for dextrin and 10 strains for fructose upon decomposition of soluble starch. Other carbohydrates were also decomposed by a few strains. 4) In an investigation of the production of alcohol and lower fatty acids, among the metabolic products detected by gas chromatography, a large amount of acetic acid and small amounts of ethanol, lactic acid, propionic acid, pyruvic acid were observed. 5) The results of enzyme activity tests using an API ZYM system indicated relatively high activities of esterase, esterase-lipase, alpha-glucosidase, alkaline phosphatase, trypsin and acid phosphatase.
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PMID:[Biological and biochemical characteristics of the oral spirochetes isolated from the focus of marginal periodontitis]. 276 48

The alterations in the distribution and activity of certain key enzymes, viz. alkaline phosphatase, acid phosphatase, glucose-6-phosphatase, cholinesterase and lipase, have been determined in the liver of rats (Rattus rattus albino) after experimental poisoning with hexavalent chromium. The histochemical and biochemical observations presented herewith provide visual evidence of chromium-induced inhibition of all these enzymes except lipase, which was found to be stimulated insignificantly. The results have been interpreted in terms of changes in the micro-environment of the cell, formation of apo-enzymes, metal-protein complexes, oxidative phosphorylation and finally with liver function.
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PMID:Dysenzymia induced by hexavalent chromium in rat liver. 299 22

Streptococcus faecalis S-48 produces a broad spectrum antibiotic, active against Gram-positive and Gram-negative bacteria. This substance is produced in solid and liquid media and also in a defined basal medium. It is sensitive to protease, pronase, or trypsin, heating at 70 degrees C, and alkaline pH, but resistant to treatment with lipase, lysozyme, alkaline phosphatase, DNAase, RNAase, acidic or neutral pHs, and also lower temperatures (60 degrees C). Several organic solvents cause precipitation, but not inactivation. This antibiotic has been partially purified by gel filtration and further ion-exchange chromatography. Its molecular weight has been estimated close to 2000. The biological activity of this antagonistic substance against the selected indicator strains, Streptococcus faecalis S-47 and Escherichia coli U-9, is bactericidal. The characterization of this substance, initially classified as a bacteriocin, indicates that it is an antibiotic of peptidic nature. The significance of antibiotic occurrence in group D of the genus Streptococcus is also discussed.
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PMID:Characterization and partial purification of a broad spectrum antibiotic AS-48 produced by Streptococcus faecalis. 309 96

The enzymatic activities of 53 strains of Pseudomonas cepacia were determined by using the API ZYM system. Strong alkaline phosphatase, acid phosphatase, butyrate esterase, caprylate esterase, myristate lipase, leucine arylamidase, and phosphoamidase activities were consistently detected in all strains. Weak activities were observed for valine arylamidase, beta-glucosidase, and N-acetyl-beta-glucosaminidase. No activities could be demonstrated for cystine arylamidase, trypsin, chymotrypsin, alpha-galactosidase, beta-galactosidase, beta-glucuronidase, alpha-glucosidase, alpha-mannosidase, and alpha-fucosidase. Enzymatic activities of pseudomonads may provide useful information about their pathogenesis and information for identification of Pseudomonas species.
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PMID:Enzymatic characterization of Pseudomonas cepacia by API ZYM profile. 335 98

The proposed system of continuous monitoring of enzyme activities is based primarily on the electrochemical behaviour of thiol compounds, and the experimental equipment is extremely simple. The determination of cholinesterase (EC 3.1.1.8) activity is described. The normal values obtained for men (73.9, s +/- 10.3 microkat/l) and for women (71.1, s +/- 10.2 microkat/l), lie within the usual range of analogous photometric methods. Systems for determination of the activities of alkaline phosphatase (EC 3.1.3.1) and adenosylhomocysteinase (EC 3.3.1.1) are described. The activity of aspartate aminotransferase (EC 2.6.1.1) is determined by a combination of enzyme reactions, in which CoA is released from acetyl-CoA. Analogous procedures are discussed for determinations of alanine aminotransferase (EC 2.6.1.2), lactate dehydrogenase (EC 1.1.1.27), lipase (EC 3.1.1.2), and phospholipase A2 (EC 3.1.1.4) activities, and for determination of substrates, e.g., acetate and carnitine. Possible determinations of an additional 199 enzyme activities and of some of substrates are suggested. By determining electrochemically active groups other than thiols this method becomes almost universally applicable.
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PMID:New system of continuous monitoring of enzyme activities and determination of some substrates. 344 Aug 58

Venoms from 20 species of stinging Hymenoptera, including nine species of ants and nine species of social wasps, were quantitatively analyzed for the following enzymic activities: phospholipase A, hyaluronidase, lipase, esterase, protease, acid phosphatase, alkaline phosphatase and phosphodiesterase. Phospholipase and hyaluronidase were present in all the venoms, with activity levels generally higher among the wasps than the ants (P less than 0.05). Lipase was present in high activity in several social wasp venoms and one ant venom, in low levels in two other ant venoms and absent from four tested snake venoms. Two-carbon esterase activity was present in the venoms of five social wasps and one ant. Non-specific protease was present at very high activity levels in the venoms of an army ant species and was also present in the venoms of a social wasp and another ant. Acid phosphatase activity was present in eight of the nine ant venoms, but was essentially absent from all the social wasp venoms. Alkaline phosphatase activity was clearly detectable in the venoms of only two species of ants. Phosphodiesterase, an enzyme not previously detected in insect venoms, was present in the venoms of three closely related ant species. Venoms with generally high enzymic activities included those of Polistes infuscatus, Vespula (V.) squamosa and Pogonomyrmex badius; those with low activities included Dolichovespula maculata, Apoica pallens and Dasymutilla lepeletierii. The 20 venoms were ranked according to overall activity levels using the eight enzyme activities plus lethal, hemolytic and pain-inducing activities. They were also compared phylogenetically using these 11 activities.
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PMID:Comparative enzymology of venoms from stinging Hymenoptera. 354 39

In a group of 58 dogs with proven pyometra, 10 bitches developed renal failure, combined with increased (p less than 0.01) urinary excretion of protein, glucose, gamma-glutamyltransferase (GGT), alkaline phosphatase (AP), amylase, lipase and casts. Thirty-two bitches without renal failure showed nevertheless signs of renal dysfunction as indicated by increased (p less than 0.01) urinary levels of protein, glucose, GGT, AP and amylase. Six bitches without significant proteinuria showed increased (p less than 0.02) urinary levels of GGT, AP as well as amylase. Thus renal injury was detected in 72 per cent of the bitches. Sixteen bitches showed normal urinary levels of protein, glucose, GGT, AP, amylase and lipase, indicating absence of renal disease.
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PMID:Renal injury in dogs with pyometra. 357 95

Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50% inhibition), independent of enzyme source, were 2-21 nM, which are about 1,000-fold lower than that of caprylohydroxamic acid, one of the most potent urease inhibitors. ATP-urea amidolyase activity was inhibited 50% by BPA at a higher concentration of 0.28 mM, but was not affected by IPA even at 1.3 mM. Thirteen kinds of hydrolases (trypsin, chymotrypsin, thermolysin, leucine aminopeptidase, papain, lipase, alpha-amylase, glucuronidase, asparaginase, arylsulfatase, alkaline phosphatase, acid phosphatase, and true cholinesterase), two oxidoreductases (catalase and alcohol dehydrogenase), three transferases (glutamic-oxaloacetic aminotransferase, gamma-glutamyl transpeptidase, and arylsulfotransferase) and two kinases (pyruvate kinase and creatine kinase) were not affected at all even at 1 mM BPA and IPA. Exceptionally, pseudo-cholinesterase from human serum was inhibited by BPA and IPA, whose I50 values were 70 nM and 10 muM, respectively, using acetylthiocholine as a substrate. These values increased to 0.55 muM and 54 muM, respectively, when acetylcholine was used as a substrate. These results show that N-acylphosphoric triamides potently and specifically inhibit urease activity at concentrations of nM order.
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PMID:Specific inhibition of urease by N-acylphosphoric triamides. 384 42

A fluorimetric assay for lipase activity has been optimized for measurement of the enzyme in human neutrophils. Activity was maximal at acid (4.5) and alkaline (9.5) pH, although there was also a neutral peak of activity at pH 6.5. Neutrophils were homogenised in isotonic sucrose and subjected to analytical subcellular fractionation by sucrose density gradient centrifugation. The gradient fractions were assayed for acid, neutral and alkaline lipase activity and for the principal organelle marker enzymes. Neutral lipase showed a unimodal distribution with an equilibrium density of 1.19 g . cm-3, corresponding to the distribution of particulate leucine aminopeptidase. Acid and alkaline lipase activities showed very similar distribution profiles to each other with both soluble components and a broad peak of particulate activity. The broad modal density of 1.19-1.22 g . cm-3 suggests that acid and alkaline lipase activities could be localised to more than one population of cytoplasmic granule. Fractionation experiments with neutrophils homogenised in sucrose medium containing digitonin confirmed the localisation of neutral lipase and leucine aminopeptidase to the same cytoplasmic granule, and suggested that at least part of the acid lipase activity was localised to the specific granule. No lipase activity could be attributed to the alkaline phosphatase-containing granule. Neutrophils were isolated from control subjects, patients with chronic granulocytic leukaemia and women in the third trimester of pregnancy. The specific activity of acid, neutral and alkaline lipase, and leucine aminopeptidase, in contrast to that of alkaline phosphatase, were similar in the three patient groups.
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PMID:Subcellular localization and properties of lipase activities in human polymorphonuclear leukocytes. 385 60


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