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)

Fluorescent Pseudomonas species (P. aeruginosa, P. fluorescens, P. putida) were tested for the presence of glycosidase activities (alpha-D-glucosidase, beta-D-glucosidase, alpha-D-galactosidase, beta-D-galactosidase, beta-xylosidase, alpha-D-mannosidase, alpha-L-fucosidase, beta-L-fucosidase, beta-D-glucuronidase and N-acetyl-beta-D-glucosaminidase). Some of the investigated glycosidases were always absent, while N-acetyl-beta-D-glucosaminidase was constantly present in all strains; 3 glycosidase activities were observed in association or separately. Serotype O11 of P. aeruginosa was found to be homogeneous with respect to some of those enzymatic activities. Search for beta-D-galactosidase, alpha-D-glucosidase and beta-D-glucosidase may be of diagnostic value in epidemiologic studies of P. aeruginosa.
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PMID:[Detection of glycosidases in Pseudomonas of the fluorescent group: relation between serotype and glycosidase activities in P. aeruginosa]. 642 62

Free beta-1, 4-glucanase activity was measured in the supernatant of cultures of Cellulomonas flavigena grown on carboxymethylcellulose or filter paper as the main carbon source. Filtration through a series of filter papers resulted in quantitative removal of the enzyme from the supernatant. The glucanase was found to be tightly bound to the paper. Cellobiose was produced from the filters containing the enzyme, when incubated at 40 degrees C. After removal of the bacterial cells the paper remnants of a C. flavigena culture also formed cellobiose. Apparently beta-1, 4-glucanase is freed into solution after the paper has been partially degraded. This release is a consequence of the decreasing ratio of cellulose to enzyme. Some glucosidase activity could be detected in the supernatant of stationary phase cultures. This was probably the result of some cell lysis. However, high activities could be measured in ultrasonic cell debris. This suggests that the beta-glucosidase of C. flavigena, contrary to beta-1, 4-glucanase, is cell-bound.
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PMID:Free and cell-bound cellulase activity of Cellulomonas flavigena. 642 84

The contamination of pollen extracts by plant matter was studied by means of enzymes. Beta-glucosidase was detected only in flowers and leaves by using the Api-Zym System. 29 pollen extracts were prepared after microscopic control. Among these 23 did not contain any plant matter and no beta-glucosidase activity could be detected. In contrast, 6 extracts were contaminated with plant matter and in every case beta-glucosidase activity was found 34 commercial pollen extracts completed the study. beta-glucosidase activity was present in 8 of them. It may be postulated that glucosidase activity detected using 2- naphthyl - beta D-glucopyranoside as a substrate, can be correlated with the presence of plant matter from the raw material from which the extract was prepared. This contamination may be important to determine since some additional sensitization may occur with such extracts during immunotherapy.
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PMID:Analysis of commercial pollen extracts by enzyme determination. II. Determination of the contamination of pollen extracts with plant matter. 642 3

A family of beta-glucosidase-stimulating proteins (called cohydrolase SPH-I here) was isolated from bovine, Gaucher human and control human spleens. All preparations exhibited a similar pattern of four major electrophoretic bands in polyacrylamide when stained with the cationic dye, Stains-All. The bovine bands migrated more rapidly, while the two types of human cohydrolase migrated very similarly. The two human preparations differed in several respects: the concentration was much higher in Gaucher spleen; the Gaucher factors eluted a little earlier from gel permeation and decyl agarose columns; much more of the cohydrolase was bound by a concanavalin A column; the control bands stained less intensely in gels than the Gaucher bands. Antibodies raised in rabbits to bovine cohydrolase reacted with all three preparations. All four bands from Gaucher cohydrolase showed similar ability to stimulate glucosidase and to bind the antibodies. It is evident that the cohydrolases from control and Gaucher spleens are similar in many respects, yet differ in some secondary fashion, possibly in carbohydrate content. It is suggested that Gaucher cohydrolase is formed from normal cohydrolase by the nonenzymatic action of cellular glucose over a period of many years, due to slowed catabolism of the cofactor.
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PMID:The cohydrolases in human spleen that stimulate glucosyl ceramide beta-glucosidase. 661 47

The present study examines the role of cardiac lysosomal enzymes in the pathogenesis of the cardiomyopathy that develops in genetically diabetic C57BL/KsJ db+/db+ mice. Db+/db+ mice and littermate controls were sacrificed as age-matched pairs between 5-26 weeks of age. C57BL/6J ob/ob mice and littermates served as other controls. The hearts were excised, homogenized, and the following enzymatic activities measured: N-Acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucosaminidase, aryl sulphatase, alpha-mannosidase, alpha-glucosidase, beta-galactosidase, beta glucosidase, total p-nitrophenyl phosphatase, acid phosphatase and 5'-phosphodiesterase type IV. There is a progressive decrease in cardiac lysosomal enzyme activities of db+/db+ mice for the period 5-21 weeks of age. All enzyme activity is depressed significantly during the 9-21 week interval with beta-glucuronidase, aryl sulphatase and beta-glucosidase decreased about 40-50%. The decrease in lysosomal enzyme activity can explain the accumulation of large residual bodies and interstitial material in the myocardium of the db+/db+ animals
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PMID:Lysosomal enzymes in experimental diabetic cardiomyopathy. 678 Feb 37

Bacteroides succinogenes S-85 grows readily in media containing 0.2% (w/v) filter paper cellulose or microcrystalline cellulose as the carbohydrate source. During growth, the cells appear to adhere to the cellulose. Cell-free culture supernates and cell extracts from cellulose-grown cultures had very low hydrolytic activity against either filter paper or crystalline cellulose (Avicel) as substrate, although H3PO4-swollen cellulose, carboxmethylcellulose, and cellobiose were readily hydrolyzed. Cells grown on either cellobiose or glucose exhibited cell-bound carboxymethylcellulase (CMCase) and cellobiase activities. Cultures grown on cellulose had seven to eight times more CMCase activity than either cellobiose- or glucose-grown cultures. Seventy percent of the CMCase activity was present in the supernate, of which 50--60% was associated with sedimentable membranous fragments. the cellobiase, which was largely cell associated, appeared to be constitutive, and the only product detected on enzymic hydrolysis of cellobiose was glucose. The cellobiase activity was strongly inhibited by 0.02 M tris(hydroxymethyl)-aminomethane (Tris), pH 7.1, but this was partially relieved by phosphate ions. These data indicate that B. succinogenes S-85 contains high endo-beta-1,4-glucanase and beta-1,4-glucanase and beta-1,4-glucosidase-like activities.
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PMID:Cellulolytic activity of the rumen bacterium Bacteroides succinogenes. 678 55

Three fluorometric leukocyte beta -glucosidase assays were compared for their ability to diagnose Gaucher's disease and identify carriers of the disorder: the acid beta-glucosidase assay of Beutler and Kuhl [2], a pH 5.5-sodium taurocholate-dependent assay and a new procedure which employs conduritol B epoxide, an active-site specific inhibitor of glucocerebrosidase. All three assays unambiguously identified patients with Gaucher's disease. With regard to identifying carriers the bile salt dependent assay of Peters et al. and the conduritol B epoxide-dependent procedure gave the greatest discrimination between the mean beta-glucosidase values for the control and heterozygote samples when evaluated using Student's t test. The most reliable assay for the identification of the carrier state was the conduritol B epoxide-dependent procedure which can be expected to provide the fewest false negative results when classifying heterozygotes (5%). However, the fact that none of these methods will completely separate control and heterozygote samples indicates that their use in screening programs will result in a significant number of incorrect assignments.
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PMID:An improved fluorometric leukocyte beta-glucosidase assay for Gaucher's disease. 679 54

beta-D-Mannosidase (beta-D-mannoside mannohydrolase EC 3.2.1.25) was purified 160-fold from crude gut-solution of Helix pomatia by three chromatographic steps and then gave a single protein band (mol. wt. 94,000) on SDS-gel electrophoresis, and three protein bands (of almost identical isoelectric points) on thin-layer isoelectric focusing. Each of these protein bands had enzyme activity. The specific activity of the purified enzyme on p-nitrophenyl beta-D-mannopyranoside was 1694 nkat/mg at 40 degrees and it was devoid of alpha-D-mannosidase, beta-D-galactosidase, 2-acetamido-2-deoxy-D-glucosidase, (1 leads to 4)-beta-D-mannanase, and (1 leads to 4)-beta-D-glucanase activities, almost devoid of alpha-D-galactosidase activity, and contaminated with less than 0.02% of beta-D-glucosidase activity. The purified enzyme had the same Km for borohydride-reduced beta-D-manno-oligosaccharides of d.p. 3-5 (12.5mM). The initial rate of hydrolysis of (1 leads to 4)-linked beta-D-manno-oligosaccharides of d.p. 2-5 and of reduced beta-D-manno-oligosaccharides of d.p. 3-5 was the same, and o-nitrophenyl, methylumbelliferyl, and naphthyl beta-D-mannopyranosides were readily hydrolysed. beta-D-Mannobiose was hydrolysed at a rate approximately 25 times that of 6(1)-alpha-D-galactosyl-beta-D-mannobiose and 6(3)-alpha-D-galactosyl-beta-D-mannotetraose, and at approximately 90 times the rate for beta-D-mannobi-itol.
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PMID:beta-D-Mannosidase from Helix pomatia. 683 86

Glucosidase activities capable of removing the three glucose residues from Glc3Man9GlcNAc2 oligosaccharide were detected in a cell-free preparation of Saccharomyces cerevisiae X-2180. The glucosidase which cleaves the glucose residue at the nonreducing terminus (Glc3Man9GlcNAc2 oligosaccharide glucosidase) was equally distributed between the particulate and the supernatant fractions obtained after centrifugation of the yeast homogenate at 27,000 X g for 30 min. The membrane-bound activity was stimulated by Triton X-100, whereas the supernatant activity was not affected. The soluble Glc3Man9GlcNAc2 oligosaccharide glucosidase was partially purified from the supernatant by ammonium sulfate fractionation followed by DEAE-Sephadex chromatography. It was clearly separated from alpha-glucosidase, which acts onp-nitrophenyl-alpha-D-glucopyranoside, but still contained beta-glucosidase and alpha-mannosidase acting on p-nitrophenyl-beta-D-glucopyranoside and alpha-D-mannopyranoside, respectively. The Glc3Man9GlcNAc2 oligosaccharide glucosidase had a pH optimum of 6.8, and showed no requirement for divalent cations. The enzyme was very active with glucose-labeled Glc3Man9GlcNAc2, was slightly active with Glc2Man9GlcNAc2, and showed no activity with Glc1Man9GlcNAc2. These properties suggest that this enzyme is involved in the first step of processing of oligosaccharides after transfer from dolichyl pyrophosphate to proteins.
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PMID:Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2. 701 69

The 105 000g supernatant from human placental homogenates, prepared in the presence of sodium taurocholate and Cutscum, contained beta-glucosidase activity towards estrone glucoside as well as towards 4-methylumbelliferyl glucoside (4-MU-glucoside) and glucocerebroside. After partial purification, the estrone glucosidase was found to be active only after the addition of negatively charged phospholipid, whereas the other beta-glucosidases did not exhibit this requirement. The estrone glucosidase was separated from the 4-MU-glucosidase by chromatography on Sephadex G-200 with 0.1% sodium taurocholate in the eluting buffer. The estrone glucosidase was mainly contained in material with a pI of 4.7, while the 4-MU-glucosidase was distributed in fractions with pI values of 4.7 and 6.2 to 6.4. The partially purified estrone glucosidase had a pH optimum of 5.8, as distinct from that of 6.4 found for the 4-MU-glucosidase, and differed markedly from the 4-MU-glucosidase in its response to treatment with heat, sulfhydryl reagents, and detergents. Its sensitivity to changes in pH differed from those reported for glucocerebrosidase.
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PMID:Estrone beta-glucosidase activity in human placenta. 738 73


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