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)

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

1. Cases of Gaucher's disease could not be distinguished from controls by the assay of beta-glucosidase activity in water homogenates of liver using 4-methylumbelliferyl-beta-D glucopyranoside. 2. Two peaks of beta-glucosidase activity were separated by Sephadex G-150 gel filtration in control and Gaucher livers. In the presence of the elution buffer pH profiles of peak I showed a deficiency at pH 3.5-4.5 in Gaucher's disease. Gaucher and control peak II had similar pH profiles with little or no activity at pH 3.0-4.0. 3. A clear distinction between homogenates of Gaucher and control liver was obtained by assay at pH 4.0 in the presence of elution buffer, or of sodium chloride, a component of the elution buffer.
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PMID:The diagnosis of Gaucher's disease in liver using 4-methylumbelliferyl-beta-D-glucopyranoside. 1 96

Variable amounts of residual 4-methylumbelliferyl-beta-glucosidase activity gave rise to difficulties in the diagnosis of Gaucher's disease using spleen and particularly liver. Soluble and particulate components of beta-glucosidase, which interfere with the diagnosis, may be eliminated by preincubation of homogenates at pH 3.0 or with 100 mM sodium chloride at pH 4.0. After either of these treatments the optimum of acid beta-glucosidase was pH 4.5 and diagnosis of Gaucher's disease could be more easily made using homogenates of spleen and liver. There was residual acid beta-glucosidase activity in one of the Gaucher livers.
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PMID:Acid beta-glucosidase and the diagnosis of Gaucher's disease in liver and spleen. 2 86

Washing skin fibroblasts or leucocytes in 0.25 mol/l sucrose increases the activity of beta-glucosidase at acid pH. This effect is primarily due to removal of low levels of sodium chloride, which inhibit acid beta-glucosidase. A secondary factor for skin fibroblasts in the removal of residual phosphate buffer pH 7.3 used to wash the cells following trypsinization. As the beta-glucosidase activity of water-lysed leucocytes is higher at acid pH than that of a saline suspension of leucocytes, the former are better for the diagnosis of Gaucher's disease. However, more reliable results still may be obtained by assay of this enzyme in cultured skin fibroblasts.
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PMID:Diagnosis of Gaucher's disease in cultured skin fibroblasts and leucocytes. 11 79

Constitutive beta-glucosidases from Saccharomyces fragilis (Y-18) and S. dobzhanskii (Y-19) precipitated at the same concentration of ammonium sulfate. The partially purified enzymes had similar activation energies, molecular weights, affinities for certain natural and synthetic beta-glucosides, and optimal pH values for substrate hydrolysis, and they were stable over approximately the same pH range. The enzymes, however, could be clearly distinguished by other criteria. Affinities of the synthetic, sulfur-containing beta-glucosides for Y-18 enzyme were many times greater than for Y-19 enzyme. The latter enzyme was more resistant to heat. The two enzymes eluted from diethylaminoethyl cellulose at different concentrations of sodium chloride. In precipitin tests, homologous enzyme-antisera systems were highly specific. The beta-glucosidase synthesized by a hybrid, S. fragilis x S. dobzhanskii (Y-42), was unique. Characterization of this enzyme produced values which were intermediate to those for the enzymes from the parental yeast strains. Heat-inactivation slopes and Lineweaver-Burk plots for the Y-42 enzyme were anomalous. It is suggested that hydrolytic activity in Y-42 preparations is due to a spectrum of hybrid enzyme molecules composed of varying amounts of two distinct polypeptides. It is further suggested that these polypeptides may be identical to those synthesized by the parental Y-18 and Y-19 yeast strains.
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PMID:Purification and characterization of yeast beta-glucosidases. 602 Apr

In observations of the movements of the infective third-stage larvae of a rodent parasitic nematode, Strongyloides ratti, on a sodium chloride gradient set up on agarose plates, two types of chemokinetic behavior were seen: a unidirectional avoidance movement on initial placement of the larvae in unfavorable environmental conditions and a random dispersal movement on their placement within an area of favorable conditions. Track patterns were straight in the avoidance movement but included multiple changes of direction and loops in the dispersal movement. In the present study we examined the interventional activity of treatment with various enzymes, lectins, and chemicals by analyzing the unidirectional avoidance movements of the larvae. We observed that beta-glucosidase, hyaluronidase, beta-galactosidase, trypsin, protease, lipase, phospholipase C, soybean agglutinin, wheat germ agglutinin, and spermidine exerted inhibitory actions on those movements, which may be guided by the chemosensory function of this nematode.
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PMID:Effects of various treatments on the chemokinetic behavior of third-stage larvae of Strongyloides ratti on a sodium chloride gradient. 1109 92

The infective third-stage larvae (L3s) of Strongyloides ratti, a parasitic nematode in rodents, showed two types of chemokinesis on a gradient of sodium chloride (NaCl) in an in vitro agarose tracking assay. The types were a consistent directional avoidance behavior under unfavorable environmental conditions and a reduced avoidance behavior under favorable conditions. We examined the effects of treatments with glycolytic enzymes and lectins by analyzing the avoidance behavior. L-Fucose dehydrogenase, hyaluronidase, beta-glucosidase, alpha-mannosidase, beta-galactosidase, concanavalin A, wheat germ agglutinin and soybean agglutinin exhibited inhibitory or enhancive effects on chemokinesis. We also confirmed the sites of the amphids of L3s aside from the mouth at the anterior end by scanning electron microscopy, and that concanavalin A-binding sites existed in the vicinity of the amphids using lectin-histochemistry. The carbohydrate moieties in the amphids of S. ratti L3s may play an important role as chemosensors in perceiving environmental cues.
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PMID:Strongyloides ratti: chemokinesis of glycolytic enzyme- and lectin-treated third-stage infective larvae in vitro. 1586 77