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)

Enhanced chemiluminescent assays for hydrolase enzymes have been developed using proenhancer and pro-anti-enhancer substrates. Alkaline phosphatase is measured using disodium para-iodophenyl phosphate (proenhancer) which is converted to para-iodophenol and this in turn enhances the light emission from the horseradish peroxidase catalysed chemiluminescent oxidation of luminol by peroxide. An alternative strategy uses para-nitrophenyl phosphate which is converted by alkaline phosphatase to para-nitrophenol which inhibits the enhanced chemiluminescent reaction. The detection limit for the enzyme using the proenhancer and pro-anti-enhancer assays was 100 attomoles and 1 picomole, respectively. The proenhancer strategy was effective in assays for beta-D-galactosidase, beta-D-glucosidase and aryl sulfatase. A limited comparison of the proenhancer and a conventional colorimetric assay for an alkaline phosphatase label in an enzyme immunoassay for alpha-fetoprotein showed good agreement.
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PMID:Chemiluminescent assay of enzymes using proenhancers and pro-anti-enhancers. 172 39

We studied strains of an unusual streptococcus that superficially resembles Streptococcus sanguis but has fibrils that are arranged in lateral tufts. These strains were originally isolated from human throats and oral cavities and have been referred to previously as "Streptococcus sanguis I," the "CR group," and the "tufted-fibril group." Until now, insufficient phenotypic data have been available to allow reliable differentiation of these strains from other viridans streptococcal species, particularly the species in the S. sanguis group. Recently, workers have proposed a scheme of phenetic tests that is based on 4-methylumbelliferyl-linked substrates and conventional biochemical tests and allows the tufted-fibril group to be differentiated; these organisms differ from other viridans species in being able to hydrolyze arginine but not esculin and in producing alpha-L-fucosidase but not beta-glucosidase or alkaline phosphatase. These data, together with the results of our DNA-DNA hybridization experiments and the unusual ultrastructure of the tufted-fibril strains as determined by electron microscopy, demonstrate that these organisms represent a new species, for which the name Streptococcus crista is proposed. The DNA base composition is 42.6 to 43.2 mol% G + C. The type strain is strain CR311 (= NCTC 12479).
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PMID:Streptococcus crista sp. nov., a viridans streptococcus with tufted fibrils, isolated from the human oral cavity and throat. 174 99

Release of PI-anchoring enzymes and other effects of phosphatidylinositol-specific phospholipase C from Bacillus thuringiensis on TN-368 cells from a moth ovary. Toxicon 27, 637-645, 1989.--The effect of phosphatidylinositol-specific phospholipase C(PIPLC) from Bacillus thuringiensis was investigated on TN-368 cells, derived from the ovary of a moth, Trichoplusia ni. Quantitative analysis of lipids showed that phosphatidylinositol (PI) was contained as one of the major phospholipids in TN-368 cells, whereas sphingomyelin and cholesterol were minor lipid components. When TN-368 cells were treated with PIPLC, significant amounts of alkaline phosphatase, 5'-nucleotidase and beta-glucosidase were released from these cells. Thus, these enzymes were shown to be PI-anchoring proteins in the plasma membrane of these cells. In the presence of 4.2 units of PIPLC, the cell growth of TN-368 was inhibited by 50%. In contrast with normal cells, the cells cultured in the presence of PIPLC became swollen and globular, losing their protoplasmic extensions. Also, there was degeneration of the interior of TN-368 cells cultivated in the presence of PIPLC. Mitochondria became swollen with a decrease in number of granules while the crista turned transparent. Also, an increase in lysosomes was observed and vacuoles seemingly derived from smooth endoplasmic reticula appeared.
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PMID:Release of PI-anchoring enzymes and other effects of phosphatidylinositol-specific phospholipase C from Bacillus thuringiensis on TN-368 cells from a moth ovary. 274 61

Male Wistar rats received a low-protein (4.5% protein) diet during 30 days, and T-2-toxin was administered to them through a gastric tube, in a dose of 0.54 mg/kg, during 15 days. The results obtained showed activation of hepatic lysosomal enzymes (sulfatase A and B aryl and beta-glucosidase) and alkaline phosphatase, and to an essential suppression of enzymatic activity of peroxisomes - catalase, glycolate oxidase and D-amino acid oxidase. A sharp aggravation of the intoxication symptoms and pronounced intensification of changes in enzymatic activity in the liver, spleen, thymus and blood serum were recorded in the animals given T-2 toxin simultaneously with the low-protein diet.
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PMID:[Enzyme parameters in the evaluation of the combined effects of protein deficiency and T-2 mycotoxin]. 289 95

The nephrotoxicity of three different dose levels of propyleneimine (10, 20 and 30 microliter/kg body wt) administered intraperitoneally to rats was studied and 20 microliters/kg body weight was found to be the most appropriate sublethal dose. Injection of propyleneimine (10 microliters/kg body wt) produced a small rise in N-acetyl-beta-D-glucosaminidase (NAG) activity, minor histological damage but no change in urine volume. Six rats were injected with 20 microliters/kg body weight, and urine was collected over the following 16 days. An immediate increase in urine volume, osmolality together with a concomitant decrease in specific gravity, was accompanied by a small increase in creatinine excretion and a more marked increase in the sodium and potassium content of urine after the administration of the nephrotoxin. NAG activity increased immediately and peaked on day 3, the activity remained elevated until day 12 when it fell to near normal levels. The activity of both beta-D-galactosidase and beta-D-glucosidase increased 9 days after administration of the nephrotoxin. In contrast, no consistent change was found in the excretion of the brush border marker enzymes, leucine aminopeptidase (LAP), alanine aminopeptidase (AAP) or alkaline phosphatase (ALP). Proteinuria increased sharply the day after injection and remained abnormal. Increased urinary albumin excretion and the predominance of low molecular weight proteins was demonstrated by sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis. Evidence is presented that propyleneimine exerts its early toxic effect on the renal papilla.
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PMID:Renal toxicity of propyleneimine: assessment by non-invasive techniques in the rat. 309 1

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

Jejunal biopsies from six patients having the small bowel enteropathy associated with common variable immunodeficiency have been subjected to analytical subcellular fractionation and enzymic and regulatory peptide microassay to define the organelle pathology of this syndrome. Compared with normal subjects, the immunodeficient patients had decreased activities of the three brush border enzymes: alkaline phosphatase, gamma-glutamyl transferase and alpha-glucosidase. The other organelle marker enzyme activities and all the regulatory peptide concentrations did not differ from the controls. Density gradient experiments showed a complete loss of particulate beta-glucosidase (lactase) with activity entirely located in the cytosol. The integrity of other organelles was normal. These data indicate that the enteropathy of common variable immunodeficiency is associated with abnormalities in the jejunal brush border analogous to those present in tropical malabsorption syndrome.
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PMID:Jejunal mucosal enzyme activities, regulatory peptides and organelle pathology of the enteropathy of common variable immunodeficiency. 369 46

The urinary excretion of N-acetyl-beta-D-glucosaminidase (NAG), beta-galactosidase (GAL), beta-glucosidase (GLU), and alkaline phosphatase (AP) was studied in 83 patients with renal allografts. Thirty of these patients had stable graft function and their urinary enzyme levels provided a range of normal values. Urinary lactic dehydrogenase (LDH) was estimated in 29 normal subjects and in 11 patients with renal allografts. Serum values for the five enzymes were also obtained. Urinary NAG excretion was abnormally high in 16 out of 17 (94%) episodes of acute rejection. The other urinary enzymes were raised less frequently. In nine patients studied before the onset of rejection urinary NAG activity rose up to three weeks before changes in other tests of renal function. Serum enzyme levels were not found to be of value in the diagnosis of rejection.
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PMID:Early warning of rejection? 457 44

1. The specific activities of beta-N-acetylglucosaminidase, acid phosphatase, alpha-mannosidase, beta-glucosidase, UDP-glucose pyrophosphorylase and alkaline phosphatase have been determined in myxamoebae of the cellular slime mould Dictyostelium discoideum Ax-2 grown on different media and in different phases of the growth cycle. 2. Variations in enzymic composition occur with changes in growth medium and phase of the growth cycle. 3. The intracellular location of the enzymes studied has been determined. 4. Two enzymes, beta-N-acetylglucosaminidase and alpha-mannosidase, are not only synthesized preferentially as the myxamoebae enter the stationary phase of growth but they are also excreted. The excretion process appears to be specific, because other enzymes that occur in the same intracellular fraction are not excreted.
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PMID:Enzyme synthesis in myxamoebae of the cellular slime mould Dictyostelium discoideum during growth in axenic culture. 467 68

1. Myxamoebae of the cellular slime mould Dictyostelium discoideum Ax-2 were grown on different media, and were harvested either in the stationary or exponential phases of the growth cycle to yield samples of myxamoebae differing in enzymic composition. 2. Morphogenesis and cell differentiation phenomena in D. discoideum appear to be similar in myxamoebae grown and harvested under different conditions. 3. The specific activity of the enzymes beta-N-acetylglucosaminidase, acid phosphatase, alpha-mannosidase, beta-glucosidase and alkaline phosphatase have been determined during cell differentiation of myxamoebae grown and harvested under different conditions. 4. The pattern of synthesis of these enzymes, all of which have been claimed to be part of the ;developmental programme', either remains unaffected despite the origin of the myxamoebae (alkaline phosphatase) or is qualitatively similar but quantitatively affected (acid phosphatase, beta-glucosidase) or is both qualitatively and quantitatively affected by changes in the myxamoebae (alpha-mannosidase, beta-N-acetylglucosaminidase). 5. The implications of these results for the concept of a ;developmental programme' are discussed.
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PMID:Enzyme synthesis in the cellular slime mould Dictyostelium discoideum during the differentiation of myxamoebae grown axenically. 467 69


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