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)

Acid hydrolases and lysosomal membrane properties were studied at various ages in the normal human brain. In CSF and four brain regions, the inferior olive, the cerebellar cortex, the caudate nucleus and the frontal cortex were thus beta-galactosidase, beta-glucosidase, alpha-mannosidase, hexosaminidase and acid phosphatase biochemically quantitated at ages varying between 2 and 89 years of age. Also the membrane latency for acid phosphatase was studied in these regions. No major regional quantitative differences were found with regard to the enzymes studied. Their kinetic properties were also defined. There appeared to exist a regional and intra-areal variation in lysosomal membrane permeability. There was, however, no age related increase in total enzyme contents. The possibility significance of these findings are discussed with reference to the aging process.
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PMID:Regional study of acid hydrolases and lysosomal membrane properties in the normal human brain at various ages. 0 May 61

Lymphocytes, monocytes, neutrophilic granulocytes and platelets were each separated to greater than 95% purity from six normal subjects, three patients with Gaucher's disease, two heterozygotes for Gaucher's disease, and one patient with Fabry's disease. Activities of the following acid hydrolases were determined: "acid" (pH 4.0) beta-glucosidase, pH 5.0 beta-glucosidase, alpha-galactosidase, alpha-arabinosidase, alpha-mannosidase, alpha-glucosidase, beta-glucuronidase, beta-galactosidase, beta-hexosaminidase, and acid phosphatase. Enzymatic activity varied greatly with cell type and the enzyme being measured; the importance of assaying pure preparations especially for heterozygote detection is emphasized. Gaucher's disease patients' cells were found to be deficient in the pH 4.0 acid beta-glucosidase, variable in the pH 5.0 beta-glucosidase, and normal in all other acid hydrolases tested, including acid phosphatase, the activity of which is known to be elevated in plasma. Blood cells of a patient with Fabry's disease were deficient in alpha-galactosidase and normal in all other acid hydrolases tested.
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PMID:Acid hydrolases in leukocytes and platelets of normal subjects and in patients with Gaucher's and Fabry's disease. 0 20

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. Highly sensitive technique are described for the assay of plasma membrane (5'-nucleotidase, alkaline phosphatase), microsomal (neutral alpha-glucosidase, leucyl-2-naphthylamidase) and biliary canalicular (gamma-glutamyltransferase) enzymes and for nine acid hydrolases (acid phosphatase, phosphodiesterase, beta-glucosidase, alpha-glucosidase, alpha-galactosidase, beta-galactosidase, alpha-mannosidase, N-acetyl-beta-glucosaminidase, beta-glucuronidase) in human liver. 2. Optimum and specific assay systems have been developed which give linear kinetics for all enzymes. 3. The range of enzyme activities in samples of human liver, obtained by closed needle biopsy, and sera have been determined.
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PMID:Enzyme activities in human liver biopsies: assay methods and activities of some lysosomal and membrane-bound enzymes in control tissue and serum. 1 4

Seven glycoside hydrolases have been investigated in suction blister fluid, interstitial fluid and in serum. Six of these have been characterized; no differences could be demonstrated between the corresponding enzymes from the various sources. The remaining enzyme (beta-glucosidase) was not found. Quantitative data suggest that 2 enzymes (beta-acetylglucosaminidase and beta-glucuronidase) diffuse freely from the epidermis into blister fluid, whereas 4 (alpha-glucosidase, alpha- and beta-galactosidase and alpha-mannosidase) are almost entirely retained in the roof of the bulla.
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PMID:Acid hydrolases in blister fluid. II. Characterization and quantification of glycoside hydrolases. 2 79

Unsubstituted naphthyl substrates were found to be superior to substituted naphthyl, indolyl and hydroxyquinoline substrates for the histochemical demonstration of alpha-mannosidase, alpha-galactosidase, hetero-beta-glycosidase, glucoamylase and sucraseisomaltase, equivalent for beta-N-acetylglucosaminidase and lactase-beta-glucosidase, and inferior for beta-glucuronidase and acid beta-galatosidase. Aldehyde fixation is necessary for the localization of lysosomal glycosidases with naphthyl substrates. 1-naphthyl substrates are suitable for the detection of acid glycosidases in lysosomes and hetero-beta-glysocidase in the cytoplasm of animal cells, and 2-naphthyl substrates can be employed for the demonstration of microvillous glycosidases and for the evaluation of the total activity of soluble glycosidases with semipermeable membranes. When naphthyl substrates are used coupling should be carried out simultaneously and hexazotized pararosaniline is the coupling reagent of choice.
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PMID:Localization of glycoidases with naphthyl substrates. 5 19

We have studied the effect of a post-translational modification mutation upon four developmentally regulated glycosidases of Dictyostelium discoideum. The presence of the modA mutation affects the intracellular level of these multimeric enzymes differently. The level of alpha-glucosidase is unaffected in the modA mutant. The mutant cell contains only a very small fraction of the wild type beta-glucosidase-1 activity. The alteration in modification renders beta-glucosidase-1 holoenzyme thermolabile and susceptible to degradation in vivo. alpha-Mannosidase-1 and N-acetylglucosaminidase are found at approximately 1/3 of the wild type level in the modA mutant. Degradation of holoenzyme does not appear to be responsible for the low level of these activities. We propose that alpha-mannosidase-1 and N-acetylglucosaminidase subunits are being degraded prior to subunit assembly. We conclude the modification bestows different properties upon the various glycosidases.
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PMID:Effects of a post-translational modification mutation on different developmentally regulated glycosidases in Dictyostelium discoideum. 9 13

The activity of several acid hydrolases in different sections of the C.N.S. of various mammalian has been evaluated. The enzymes which have been studied are: beta-glucosidase, beta-galactosidase, beta-N-acetylglucosaminidase, beta-N-acetylgalactosaminidase, beta-glucuronidase, alpha-mannosidase. The enzymes show a higher activity in the gray matter than in the white matter. The results are interpreted on the assumption that glyco-lipoprotein turnover is higher in the gray matter than in the white matter, since myelin, which is the major component of the white matter, is a relatively stable structures.
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PMID:[Behavior of certain acid hydrolases in the central nervous systems of various mammals]. 16 40

Rats bearing Reuber H-35 or Novikoff hepatomas and mice bearing L1210 or L5178Y murine leukemias exhibited elevated serum levels of fetuin : N-acetylneuraminic acid transferase (EC 2.4.99.1) activity. The serum transferase activity could be correlated with the growth rate of the tumor; in animals bearing the more rapidly growing Novikoff hepatoma, activity was higher than in animals bearing the Reuber H-35 hepatoma. Higher transferase levels were also found in L1210 leukemic mice than in mice with the slightly slower growing L5178Y leukemia. Serum from rats bearing Reuber H-35 hepatoma and mice bearing L1210 murine leukemia had elevated levels of alpha- and beta-glucosidase (EC 3.2.1.20 and EC 3.2.1.21), alpha- and beta-galactosidase (EC 3.2.1.22 and (3.2.1.23), beta mannosidase (EC 3.2.1.25), alpha- and beta-fucosidase (EC 3.2.1.- and EC 3.2.1.38), beta-N-acetylglucosaminidase (EC 3.2.1.30) and acid phosphatase (EC 3.1.3.2); alpha-mannosidase (EC 3.2.1.24), beta-N-acetylgalactosaminidase (EC 3.2.2.-) and beta-xylosidase (EC 3.2.1.37) were not elevated. In animals bearing Reuber H-35 hepatoma, host liver levels of glycosidases, beta-glucuronidase (EC 3.2.1.31) and acid phosphatase were elevated over both the control and the hepatoma values. The data are interpreted to mean that the tumors or various host tissues release large quantities of enzymes into the serum and that enzyme levels in host organs may also be affected by the tumor.
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PMID:Serum and host liver activities of glycosidases and sialyltransferases in animals bearing transplantable tumors. 17 98

The P4 variant of Dictyostelium discoideum is characterized by the production of fruiting structures in which the overall proportion of stalk to spore material is increased, relative to the wild type. The altered morphology of the mutant is due to increased sensitivity to cyclic AMP which promotes stalk cell differentiation. In the presence of 10-4 M-cyclic AMP the entire population of P4 amoebae forms clumps of stalk cells on the surface of the dialysis membrane support. Measurement of changes in activity of a range of developmentally-regulated enzymes during the development of P4 in the presence and absence of cyclic AMP has allowed us to identify three classes of enzyme: (i) Those, such as beta-glucosidase II, trehalose-6-phosphate synthetase and uridine diphosphogalactose-4-epimerase, which are required for the production of spores. (ii) Enzymes, primarily but perhaps not exclusively, required during stalk cell formation. Typical of these are N-acetylglucosaminidase and alkaline phosphatase. (iii) General enzymes, such as threonine dehydrase, alpha-mannosidase and uridine diphosphoglucose pyrophyosphorylase, which are present inboth pre-stalk and pre-spore cells and appear to be necessary for the development of both cell types.
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PMID:Enzyme activity changes during cyclic AMP-induced stalk cell differentiation in P4, a variant of Dictyostelium discoideum. 17 91


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