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)

Using fully mechanized analytical equipment, interference by haemolysis in the determination of 26 clinical chemical parameters was determined quantitatively by adding haemolysate to serum. Haemoglobin concentrations up to 6.6 g/l caused essentially no interference in the following determinations: albumin (immuno-nephelometric), alpha-amylase, calcium, chloride, cholesterol, cholinesterase, creatinine, iron, glucose, glutamate dehydrogenase, uric acid, urea, sodium, inorganic phosphate, total protein, transferrin and triglycerides. In the presence of haemoglobin, erroneously high values were found for: lactate dehydrogenase (haemoglobin higher than 0.2 g/l), aspartate aminotransferase, potassium and acid phosphate (haemoglobin higher than 1.5 g/l), creatine kinase (haemoglobin higher than 2.5 g/l) and alanine aminotransferase (haemoglobin higher than 3.4 g/l). Erroneously low values were found for bilirubin (haemoglobin higher than 0.8 g/l), alkaline phosphatase and albumin (by electrophoresis) (haemoglobin higher than 1.5 g/l) and gamma-glutamyltransferase (haemoglobin higher than 3.0 g/l).
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PMID:Haemolysis as an interference factor in clinical chemistry. 371 97

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

Simultaneous determination of pancreatic proteases, alpha-amylase, lactase and alkaline phosphatase in 2-, 6- and 28-month rats showed deep alterations on the level of cavitary and membrane digestion. Total hydrolytic potential for proteins and carbohydrates is rather high in growing rats and gradually reduces in old animals. These alterations in growing animals are mainly actualized through the small intestine enzymes while in adolescent and old rats - through the pancreatic enzyme systems.
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PMID:[Enzyme systems of intraluminal and membrane hydrolysis of food substances in growing, adult and old rats]. 390 18

We analyzed the stability of the enzymes alpha-amylase (EC 3.2.1.1), alkaline phosphatase (EC 3.1.3.1), alanine aminotransferase (EC 2.6.1.2), aspartate aminotransferase (EC 2.6.1.1), creatine kinase (EC 2.7.3.2), glutamate dehydrogenase (EC 1.4.1.3), gamma-glutamyltransferase (EC 2.3.2.2) and lactate dehydrogenase (EC 1.1.1.27) of a human serum pool during storage in liquid nitrogen for a period of 10 months. Except amylase and creatine kinase, all enzymes were stable. Amylase increased in activity, creatine kinase activity decreased. Therefore, human serum stored at -196 degrees C can be used as satisfactory substitute for lyophilized enzyme control serum in internal quality control and stable enzyme material for optimization of methods.
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PMID:Long-term stability of enzymes in human serum stored in liquid nitrogen. 614 44

In tissue decalcified with MgNa2EDTA at a neutral pH activity for ATPase can used be for demonstration of the vascular structures at the muscle-bone interface. The GOMORI method for alkaline phosphatase is only of value, when fresh unfixed tissue is to be examined. The azo-dye method for alkaline phosphatase failed to give satisfactory results, and so did the alpha-amylase PAS method. 5'-nucleotidase activity is present in both capillaries and in cells lining the surfaces of bones, while larger blood vessels are poorly stained.
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PMID:Methods for histochemical demonstration of vascular structures at the muscle-bone interface from cryostate sections of demineralized tissue. 616 24

An alpha-amylase gene from Bacillus coagulans has previously been cloned in Escherichia coli and shown to direct the synthesis of an enzymically active protein of 60,000 Dal (Cornelis et al., 1982). In one particular E. coli host, strain HB101, amylase was found to accumulate in the periplasmic space. To study the processing and the location of the amylase, plasmid pAMY2 was introduced into E. coli 188 which is a strain constitutive for alkaline phosphatase, a periplasmic marker, and for beta-galactosidase, a cytoplasmic marker. Abnormally large amounts of both alpha-amylase and beta-galactosidase were found in the culture fluid of cells grown in rich medium. Furthermore a severe growth defect was found when cells containing pAMY2 were grown in maltose and glycerol media, while the ability to grow on glucose remained normal. This defect could be reversed by two types of spontaneous mutations. Mutations in the first class are located on the plasmid and correspond to the insertional inactivation of the amylase gene by IS1. Mutations in the second class are located on the host chromosome. These results suggest that the synthesis and export of B. coagulans alpha-amylase is deleterious to E. coli, especially in media containing maltose or glycerol as sole carbon source.
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PMID:Growth defects of Escherichia coli cells which contain the gene of an alpha-amylase from Bacillus coagulans on a multicopy plasmid. 618 99

It has been demonstrated by the methods of histochemical and biochemical examination of the activity of the enzymes that the mucus layer covering the small intestinal wall contains active enzymes (alkaline phosphatase, leucin aminopeptidase IV, saccharase, lactase) and pancreatic enzymes (alpha-amylase and trypsin). Emphasis is laid on the enrichment of the mucus layer with pancreatic enzymes as compared with small intestinal juice. A hypothesis has been advanced according to which the mucus layer undergoes degradation of polymeric and oligomeric substrates, which plays a physiological part in the digestion of nutritive substances and protection of the internal medium against immunoactive biopolymers. The digestion occurring in the mucus layer is proposed to be called mucus digestion.
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PMID:[Enzymes in the mucosal layer of the small intestine]. 619 54

Activities of alpha-hydroxybutyrate- and lactate dehydrogenases (HBDH, LDH), aspartate- and alanine aminotransferases (AST, ALT), alkaline phosphatase, alpha-amylase as well as content of total proteins, glucose, cholesterol, triglycerides and Ca2+ were estimated sprectrophotometrically in blood serum of rat males within 2 hrs after thermic burns of the III degree involving 15% the body surface. The burns caused about 2-fold increase in activities of LDH, HBDH and AST and in content of triglycerides in blood serum but did not affect the other biochemical patterns. Adrenalectomy, carried out within 3 days before the burns, accelerated and pseudoadrenalectomy decreased the early postburn enzymatic activation. Preadministration of reserpine, phentolamine and obsidane (propranolol) decreased distinctly the hyperenzymic reaction observed after the burn stress.
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PMID:[Effect of adrenalectomy and anti-adrenergic preparations on the development of hyperenzymic and biochemical changes in the blood in burns]. 620 53

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

Purpura was grossly observable in albino mice 6 to 8 h after the intraperitoneal injection of sterile, deoxyribonuclease-treated, cell-free extracts prepared by sodium deoxycholate-induced lysis, sonic disruption, Parr bomb treatment, autolysis without sodium deoxycholate, or alternate freezing and thawing of washed suspensions of Streptococcus pneumoniae type I. Cell-free extracts obtained from sonically disrupted, heat-killed cells (100 degrees C for 20 min) did not contain purpurogenic activity. The reaction was maximal at approximately 24 h postinjection, started to fade slowly after 24 to 48 h, and usually was not grossly observable by 4 to 6 days postinjection. The purpura-producing principle (PPP) in the cell-free extract was purified by sequential ammonium sulfate precipitation, protamine sulfate precipitation, Sepharose 6B gel filtration, wheat germ lectin-Sepharose 6MB affinity chromatography, ribonuclease and trypsin treatment, and a second Sepharose 6B gel filtration step. The final preparation (i) contained glucosamine (5.6%), muramic acid (8.0%), neutral carbohydrate (12.8%), phosphate (8.0%), orcinol-reactive material (6.0%), and Lowry-reactive material (1.6%), and (ii) was free of detectable amounts of deoxyribonucleic acid, capsular polysaccharide, neuraminidase, cytolysin, and hyaluronidase. The isoelectric point and molecular size of the PPP were approximately pI 3.0 and several million daltons, respectively, and the activity remained in the supernatant fluid after centrifugation for 1 day at 105,000 x g. PPP activity was destroyed by incubation with egg white lysozyme and sodium metaperiodate but was resistant to trypsin, pronase, alpha-amylase, deoxyribonuclease, ribonuclease, alkaline phosphatase, pancreatic lipase, 7% trichloroacetic acid, 6 M urea, autoclaving (121 degrees C) for 30 min, and mild acid and alkali exposure. Our observations indicate that the PPP requires intact beta-1,4-glucosidic linkages for activity and support the working hypothesis that activity is associated with pneumococcal peptidoglycan solubilized by the bacterium's autolysin.
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PMID:Characterization of pneumococcal purpura-producing principle. 624 53


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