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)

174 patients with chronic pancreatic diseases, 30 patients with pancreatic carcinoma and 144 with chronic relapsing pancreatitis, 50 of them with calcifications, were observed in the Department of Internal Medicine of the University of Marburg/FRG between 1972 and 1982. In order to differentiate between carcinoma and relapsing pancreatitis the data of these patients were analysed retrospectively with regard to patient history, actual complaints, findings of laboratory, sonography, ERCP and X-ray investigations. The following results were obtained: Of discriminating value are steatorrhoe, local palpatory pain, alcohol ingestion, a history of earlier attacks and relapsing pain situations; however, general abdominal pain, nausea, vomiting and weight loss (if not exactly specified) are not. Within the laboratory findings bilirubin, GOT, alkaline phosphatase, gamma-GT, serum potassium, blood sugar and chymotrypsin content of the stool were significant while serum and urine amylase were similarly distributed within the groups of patients. Carcinoma and chronic relapsing pancreatitis can be identified by sonography in the majority of patients, but calcifications of the pancreas were rarely demonstrated during this observation period. The obstruction of the extrahepatic bile ducts--mostly due to a carcinoma of the pancreas head--was usually well documented by sonography. Intraabdominal air proofed to be the most disturbing factor. In carcinoma patients, the ERCP is important in demonstrating a complete obstruction of the pancreatic duct and stenosis and dilatation of the extrahepatic bile ducts. In patients with chronic relapsing pancreatitis the pancreatic duct alterations such as dilatations and partial stenosis are well documented by ERCP especially if calcifications occur. In patients without calcifications, dilatation of the branches of the main duct are less relevant in the diagnosis of pancreatic diseases. Radiological demonstration of calcification of the pancreatic area is important for the differential diagnosis. Longstanding characteristical complaints, symptoms and calcifications within the pancreatic area are the most relevant factors in discriminating carcinoma and chronic relapsing pancreatitis.
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PMID:[Differential diagnostic evaluation of chronic pancreatitis in relation to pancreatic cancer based on clinical, laboratory chemical and diagnostic parameters. Studies of 174 patients in 10 years]. 353 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

The quantitative release of enterokinase from isolated rat enterocytes following treatment with taurocholate-taurodeoxycholate, papain, chymotrypsin, elastase, carbamylcholine, and cholecystokinin-octapeptide was examined. Alkaline phosphatase and lactate dehydrogenase activities were evaluated simultaneously to check for specificity. Bile salts promoted a concentration-dependent release of all enzymes. Concomitantly, bile salts also led to cell destruction in proportion to the amount of enzymes released. Proteases caused the release of enterokinase and alkaline phosphatase with no concomitant increase of lactate dehydrogenase or cell lysis. At equal concentrations, papain released more enzymes than chymotrypsin and elastase. Chymotrypsin and elastase, however, led to higher ratios of enterokinase to alkaline phosphatase found in the media and suggested a selective release of enterokinase (EK) over that of alkaline phosphatase. Bile salts and pancreatic proteases together seem to have an additive effect of the release of EK. Carbamylcholine and cholecystokinin-octapeptide had no effect on enzyme release. These results suggested that pancreatic proteases are involved in the release of enterokinase by a selective action. Bile salts may also play a role through a nonselective detergent effect.
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PMID:Physiological factors controlling release of enterokinase from rat enterocytes. 390 6

The enzymatic profiles of 109 clinical isolates of Acinetobacter calcoaceticus subsp. anitratus and lwoffi were determined with conventional plate tests and the rapid API ZYM system (Analytab Products, Plainview, N.Y.). The majority of strains tested lacked DNase, hemolysin, protease, elastase and gelatinase. Strong enzymatic activities of butyrate esterase (C4), caprylate esterase (C8) and leucine arylamidase were detected in all isolates. No trypsin, chymotrypsin, alkaline phosphatase or glucosidase activities were present. This profile was characteristic of all isolates examined by the API ZYM system and could serve as a useful diagnostic feature of Acinetobacter calcoaceticus subsp. anitratus and subsp. lwoffi.
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PMID:Enzymatic profile of clinical isolates of Acinetobacter calcoaceticus. 400 64

1. The action of beryllium on the following enzymes has been examined: alkaline phosphatase (Escherichia coli and kidney), acid phosphatase, phosphoprotein phosphatase, apyrase (potato), adenosine triphosphatase (liver nuclei, liver mitochondria, brain microsomes), glucose 6-phosphatase, polysaccharide phosphorylases a and b, phosphoglucomutase, hexokinase, phosphoglyceromutase, ribonuclease, A-esterase (rabbit serum), cholinesterase (horse serum), chymotrypsin. Alkaline phosphatase and phosphoglucomutase are inhibited by 1mum-beryllium sulphate whereas the other enzymes are largely unaffected by 1mm-beryllium sulphate. 2. Possible mechanisms for the inhibition of phosphoglucomutase and alkaline phosphatase are discussed.
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PMID:The inhibition of enzymes by beryllium. 428 87

An enzyme isolated from Aerobacter aerogenes acts both as phosphomonoesterase and phosphotransferase with glucose, glucosides, glucosamine, and N-acetyl glucosamine as acceptors. When glucose-6-phosphate is the phosphate donor, these acceptors appear to act as activators of the enzyme, while with p-nitrophenyl phosphate, alpha-glycerophosphate, fructose-1,6-diphosphate, and several other phosphate esters as donors, the same acceptors act as noncompetitive inhibitors. With p-nitrophenyl phosphate as the phosphate donor, no inhibition is observed when glucose is replaced as acceptor by 2-deoxy glucose. The inhibition by glucose and other acceptors is eliminated at low pH or by increasing the temperature of reaction. Partial proteolysis of the enzyme by chymotrypsin produces a modified enzyme (gl-phosphotransferase-Ch) that shows altered relative velocities for the hydrolysis of several substrates as well as altered regulatory effects by acceptors.
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PMID:Regulatory effects of substrates on a phosphotransferase from Aerobacter aerogenes and modification of its activity by partial proteolysis. 525 17

The cytoplasmic membrane of Mycoplasma laidlawii strain B is solubilized by anionic and nonionic detergents, succinylation, phospholipase A, alkaline phosphatase, trypsin, and chymotrypsin. Cationic detergents are without effect, as are chelating agents, even in the presence of high concentrations of monovalent cation. The detergent-solubilized membrane exhibits one peak in the analytical ultracentrifuge, but the sedimentation coefficient is dependent upon concentration of detergent. Simple dialysis does not remove all of the sodium dodecylsulfate except from lipid-depleted membrane particles. Membranes bind sodium dodecylsulfate but acetone powders of membranes do not. Sulfated alcohols with chain lengths of C(14) and C(16) are more tightly bound than dodecylsulfate. A constant amount of di- and trivalent cation is bound by the membrane upon aggregation. Only a portion of this cation is removable with chelating agents. No chelating agent is bound by these aggregates. A portion of the lipid-depleted membrane particles is solubilized by negatively charged lipids and detergents, giving rise to aggregates in the presence of divalent cation. Fractionations of detergent-solubilized membranes by preparative gel electrophoresis and ammonium sulfate were inconclusive. Density gradient centrifugation of succinylated membranes yielded at least five fractions which exhibited homogeneity by ultracentrifugation. Analytical gel electrophoresis of these fractions demonstrated heterogeneity. The composition of these five fractions suggested separation of protein from lipid.
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PMID:Observations on membranes of Mycoplasma laidlawii strain B. 536 Dec 9

Rat pancreases were minced and treated with collagenase or collagenase supplemented with chymotrypsin to yield a mixture of ducts, islets, acinar cell clusters, blood vessels, and nerves. Histologically and ultrastructurally, the isolated tissues resembled their in situ counterparts in most respects, the major difference being the destruction of the basement membranes (basal laminae). Ducts ranging in size from the common bile/main pancreatic duct to the intercalated ducts were identified in the digest, although interlobular ducts were most frequently observed. Acinar tissue fragments were separated from nonacinar structures either by flotation through discontinuous gradients of Ficoll or by sieving, the latter technique being the more efficient. Common bile/main ducts, interlobular ducts, and blood vessels were selected manually from the nonacinar fractions. Biochemical analyses showed that the entire nonacinar fraction, as well as isolated ducts and blood vessels, contained larger alkaline phosphatase, carbonic anhydrase, and Mg-ATPase specific activities than acinar tissue, whereas acinar tissue contained larger gamma-glutamyltranspeptidase and amylase activities. However, greater than 63% of the total recovered activity of each enzyme was associated with the acinar tissue. Both the association of the majority of each of these enzyme activities with the acinar tissue and the similarity in specific activities associated with ducts and blood vessels indicate that none of the enzymes tested is a unique marker for interlobular and larger ducts of the pancreas of the rat.
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PMID:Characterization of ducts isolated from the pancreas of the rat. 615 56

Rat and hamster pancreatic ducts were isolated by digestion with collagenase plus chymotrypsin and were cultured for eight weeks in an agarose matrix. Freshly isolated and cultured ducts were characterized morphologically and biochemically. The in vivo morphology of the ducts was maintained in vitro, although certain differences were noted. Both interlobular and intralobular ducts could be identified. gamma-Glutamyltranspeptidase and Mg-ATPase were stable enzymatic activities of the ducts of both species; alkaline phosphatase persisted only in the hamster ducts. Carbonic anhydrase and (Na + K)ATPase were minor activities of the rat ducts. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the rat ducts suggested that actin was the major duct peptide and that the major zymogens were greatly diminished. These results demonstrate that pancreatic ducts can be maintained in vitro and can be used for biochemical studies of this minor pancreatic tissue type.
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PMID:Morphologic and biochemical characteristics of isolated and cultured pancreatic ducts. 616 52

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


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