Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Optimal assay conditions are described for 8 hydrolases of Euglena gracilis var. bacillaris, SM-L1 (streptomycin-bleached) strain, 7 of which have an acid pH-optimum. Acid-phosphatase, beta-galactosidase, beta-glucosidase, b-fucosidase, cathepsin D, RNase, DNase, and an esterase are active in cell homogenates. Amylase has very low activity, and beta-glucuronidase, arylsulfatase, beta, N-acetyl-glucosaminidase, alpha-fucosidase, and alpha- and beta-mannosidase are inactive.
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PMID:Hydrolytic enzymes of Euglena gracilis: characterization and activity as a function of culture age and carbon deprivation. 0 4

The optimal reaction conditions and kinetic properties of eleven leukocyte acid hydrolases determined with the use of fluorigenic derivatives of 4-methyl-umbelliferone are described. The enzymes studied were acid phosphatase, aryl sulfatase, alpha- and beta-glucosidase, alpha- and beta-galactosidase, alpha-mannosidase, N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucuronidase and alpha-fucosidase. More than 90% of the activity of each enzyme was released into a 27,000 X g supernatant by a double sonication procedure employing 0.9% sodium chloride and 0.1% Triton X-100. The Km values obtained were similar to those previously reported for chromogenic subtrates. A single Km value could not be derived for beta-galactosidase because its double reciprocal plot was not linear. All enzymes could be measured with less than 10 mug of protein within 15 min. Activators and inhibitors studied included the chloride salts of Na+, K+, Zn2+, Ca2+, Mg2+, Hg2+, and Fe2+ as well as p-chloromercuriphenysulfonate, glutathione, BAL, EDTA, EGTA, Triton X-100 and sodium taurocholate. The reaction conditions described in this report can be used for the diagnosis of various lysosomal storage diseases and should facilitate the development of automated procedures for the analysis of these eleven enzyme activities with small quantities of blood.
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PMID:Human leukocyte acid hydrolases: characterization of eleven lysosomal enzymes and study of reaction conditions for their automated analysis. 0 26

The paper describes a number of tests for the rapid detection of glycosidases including alpha-glucosidase, beta-glucosidase, beta-glucuronidase, beta-xylosidase and alpha-fucosidase. The methods use heavy suspensions of viable but non-multiplying bacteria in a buffered solution of a chromogenic substrate. The results of the tests are readable within 4 h. The application of these tests to a collection of 633 strains of Enterobacteriaceae and Vibrionaceae demonstrates that some of the tests may be valuable additions to the present tests available for the identification of bacteria belonging to these families. beta-glucuronidase activity was observed only in strains of the Escherichia-Shigella group. 97 per cent of the Escherichia strains possessed beta-glucuronidase activity. beta-xylosidase activity was almost completely restricted to strains of the Klebsiella-Enterobacter group in addition to Yersinia strains. None of the strains possessed alpha-fucosidase activity.
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PMID:Rapid diagnosis of Enterobacteriaceae. I. Detection of bacterial glycosidases. 0 74

This paper deals with the measurement of acid hydrolases in uncentrifuged and centrifuged saliva of normal controls and the determination of some of their physical characteristics such as pH optimum, thermal stability, and residual activity after freezing and storage. From this study it appears that beta-D-glucosidase sediments totally, whereas the other enzymes show varying residual activity in the supernatant after centrifugation. In the saliva from 2 patients with metachromatic leukodystrophy and 2 patients with fucosidosis a deficiency of arylsulphatase A and alpha-L-fucosidase, respectively, was found.
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PMID:Determination of lysosomal enzymes in saliva. Confirmation of the diagnosis of metachromatic leukodystrophy and fucosidosis by enzyme analysis. 4 Jul 13

1. The elution profiles of eleven acid hydrolases from human liver and plasma were directly compared using a system whereby a single salt gradient was simultaneously applied to two DEAE-cellulose chromatographic columns. 2. Plasma alpha-L-fucosidase, alpha-mannosidase, alpha-galactosidase and alpha-glucosidase isoenzymes were eluted at higher salt concentrations than the corresponding liver isoenzymes whereasbeta-N-acetylglucosaminidase, beta-galactosidase, beta-glucosidase, exo-1,4-beta-xylosidase and alpha-L-arabinofuranosidase isoenzymes were eluted at lower salt concentrations. The elution profiles of beta-glucuronidase and acid phosphatase weremore complex. 3. After incubation with neuraminidase most plasma hydrolases were eluted at lower salt concentrations, however the elution patterns of beta-glucosidase, beta-xylosidase and acid phosphatase were not altered. 4. Preincubation with neuraminidase had no effect on the elution profiles of six liver hydrolases whereas the major isoenzymes of alpha-mannosidase, beta-galactosidase and alpha-L-arabinofuranosidase were eluted at markedly lower salt concentrations. Liver alpha-fucosidase and alpha-galactosidase were eluted at slightly lower salt concentrations afterincubation with neuraminidase. 5. The results are discussed in relation to thepathogenesis of Mucolipidosis II (I-cell disease), and the synthesis and packaging of lysosomal enzymes.
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PMID:Effect of neuraminidase on the chromatographic behaviour of eleven acid hydrolases from human liver and plasma. 19 Dec 58

This is a review of the properties and molecular genetics of six lysosomal hydrolases: beta-galactosidase, hexosaminidases A and B, alpha-galactosidase, beta-glucosidase and alpha-fucosidase. Each enzyme is discussed with regards to isoenzymes and substrate specificity, subunit structure, genetic relationship of isoenzymes and genetic variants. The molecular genetics of human diseases caused by deficiencies of each enzyme are discussed.
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PMID:Glycosphingolipid hydrolases: properties and molecular genetics. 20 Aug 37

1. Six weeks after the injection of streptozotocin at 125 mg/kg i.p. in the AV line nondiabetic Chinese hamsters, the animals showed hyperglycemia, increased kidney, pancreas and stomach weights and stomach glucagon contents and depletion of insulin and glucagon in the pancreas. 2. Plasma beta-D-galactosidase and N-acetyl-beta-D-glucosaminidase were elevated; whereas alpha-D-glucosidase was decreased and alpha-D-galactosidase remained unchanged in the plasma. 3. In the kidney, streptozotocin-diabetes led to depression of alpha-D-mannosidase, beta-D-fucosidase and N-acetyl-beta-D-glucosaminidase activities in both 12,000 g supernatant and precipitate fractions, decreases in alpha-D-glucosidase in the supernatant only and no change in alpha-L-fucosidase, alpha-D-galactosidase, beta-D-galactosidase and beta-D-glucuronidase. 4. In the liver, significant increases in N-acetyl-beta-D-glucosaminidase, alpha-D-galactosidase, beta-D-galactosidase, beta-D-fucosidase, beta-D-glucosidase and alpha-D-mannosidase were found in either the supernatant or the precipitate fraction of the diabetic animals. The data indicate diabetes-dependent tissue-specific changes in glycohydrolases in the Chinese hamster.
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PMID:Alterations in glycohydrolase activities in streptozotocin-diabetic Chinese hamsters (Cricetulus griseus). 31 16

The activities of 9 acid hydrolases were determined in cell-free amniotic fluid, leucocytes and cultured fibroblasts using fluorogenic substrates. The specific activities of beta-glucosidase, alpha-fucosidase, beta-hexosaminidase, and arylsulphatase A and B were found to be in the same range in cell-free amniotic fluid and in leucocyties. The isoenzyme pattern of these 5 hydrolases as well as that of acid phosphatase and alpha-mannosidase showed some similarities in all three specimens studied; the pattern of alpha- and beta-galactosidase obtained by isoelectric focusing was different in the 2 types of cells studied and in the cell-free amniotic fluid.
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PMID:Isoelectric focusing pattern of acid hydrolases in cultured fibroblasts, leucocytes and cell-free amniotic fluid. 57 95

The pH optima and apparent Km and Vmax values were determined for nine glycosidases of the retinal pigment epithelium (RPE) of the calf. In terms of micromoles of substrate cleaved per milligram protein per hour, the following relative order of enzymatic activities was observed: beta-N-acetylglucosaminidase greater than alpha-glucosidase = beta-N-acetylgalactosaminidase greater than alpha-mannosidase greater than beta-galactosidase greater than beta-glucosidase greater than alpha-fucosidase greater than alpha-galactosidase greater than beta-glucuronidase. The pH optimum of each of these enzymes was in the acidic range (below pH 6). All these findings refer to enzymatic activities of bovine RPE preparations obtained by the brushing procedure of Glocklin and Potts and washing as described by Berman and Feeney. Thus they may relate to those activities associated with particulate components of the RPE cell and not to the more soluble glycosidases. The distribution of the glycosidases between the washes of the cells and the final pellet of bovine RPE cells was examined. The activities of 10 glycosidases in the RPE of the embryonic chick were also examined. Neither beta-mannosidase nor beta-fucosidase activities could be detected in washed bovine RPE cells, although beta-mannosidase was detected in RPE of the embryonic chick. The presence of isoenzymes of beta-glucuronidase in bovine RPE was indicated. Specificity by beta-glucuronidase of bovine RPE for synthetic substrates was observed.
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PMID:Glycosidases of the retinal pigment epithelium. 70 Sep 67

In comparison with 1- and 2-naphthyl beta-D-glucoside, beta-D-galactoside, beta-D-glucuronide, beta-D-N-acetylglucosaminide, alpha-D-glucoside, alpha-D-galactoside and alpha-D-mannoside 1- and 2-naphthyl alpha-L-fucoside are hydrolyzed more quickly or to the same extent by homogenates prepared from freeze-dried cryostate sections of various rat organs. Nevertheless, when the fucosides are employed for the histochemical demonstration of alpha-L-fucosidase mostly negative data were obtained independent on the method used, whereas all other naphthyl glycosies deliver positive results. The reasons for these discrepancies are the marked inhibition of alpha-L-fucosidase by aldehyde fixation and diazonium salts. Then, alpha-L-fucosidase activity is suppressed to 90% and between 85 and 98% respectively; the inhibition of alpha- and beta-D-glucosidase, alpha- and beta-D-galactosidase, alpha-D-mannosidase, beta-D-glucuronidase and beta-D-N-acetylglucosaminidase by the fixative or coupling reagent does not exceed 70%. Therefore 1- and 2-naphthyl alpha-L-fucoside cannot be recommended in general for histochemical purposes. Small amounts of dimethylformamide do not influence the activity of most of the glycosidases investigated. For biochemical measurements, however, especially 1-naphthyl alpha-L-fucoside represents a suitable alternative in a fluorometric procedure instead of p-nitrophenyl alpha-L-fucoside used for the photometric evaluation of alpha-L-fucosidase. With the fluorometric method the enzyme was measured in rat organs, which posses remarkably different activities of alpha-L-fucosidase.
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PMID:[Suitability of naphthyl-alpha-L-fucosides for the investigation of alpha-L-fucosidases (author's transl)]. 88 38


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