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)

beta-glucosidase, cellulase, alpha-mannosidase, beta-galactosidase, and N-acetyl-beta-glucosaminidase were tested for their ability to hydrolyse the carboxymethylcellulose contained in 'Rely' tampons (R-CMC). The end-products of the hydrolysis were determined by chromatography. Only beta-glucosidase and cellulase hydrolysed R-CMC and the major product detectable after enzymic degradation was glucose, as confirmed chromatographically and by the glucose oxidase test. The enzymic-degradation products of R-CMC were able to support the growth of a toxic-shock-syndrome strain of Staphylococcus aureus. This finding suggests that as it is degraded by enzymes in the vaginal cavity R-CMC may become an exogenous source of nutrients for pathogenic organisms.
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PMID:Growth of toxic-shock-syndrome strain of Staphylococcus aureus after enzymic degradation of 'Rely' tampon component. 613 1

Glycosidase activities in the adults and juveniles of the lung fluke Paragonimus ohirai and P. westermani adults were demonstrated histochemically. For comparative studies, histochemical examination was also made on the adults of the liver fluke Fasciola hepatica. The enzymes examined were N-acetyl-beta-glucosaminidase (EC 3.2.1.30), beta-glucuronidase (EC 3.2.1.31), beta-galactosidase (EC 3.2.1.23), alpha-glucosidase (EC 3.2.1.20) and beta-glucosidase (EC 3.2.1.21). The distribution of beta-glucosaminidase was similar in juveniles and adults. Strong reaction sites for the enzyme were the caecal brush border, tegument, subtegumental cells and tests. In contrast, no staining reaction occurred in the caeca of F. hepatica, although the tegument and parenchymal cells were weakly stained. beta-glucuronidase activity was associated only with the luminal surface of the caeca in the juveniles. However, luminal contents also appeared stained and this might suggest that the activity in the caeca is not endogenous. beta-galactosidase was localized in the caeca, sub-tegmental cells and tegument in both juveniles and adults. No reaction occurred for the other two enzymes, alpha- and beta-glucosidase.
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PMID:Histochemical studies of glycosidase activity in juveniles and adults of the lung fluke Paragonimus. 622 Feb 58

Changes in the activities of several lysosomal enzymes were studied during transformation of mouse spleen cells in vitro. The activity of beta-glucuronidase increased during culture in the presence of T or B-cell mitogens, and lymphoblasts contained higher levels of activity than did small, non-transformed lymphocytes. Moreover, lymphoblasts in well-transformed cultures had higher activities than those in poorly-transformed cultures. The activities of other lysosomal enzymes (N-acetyl-beta-glucosaminidase, alpha-mannosidase, beta-glucosidase) also increased during mitogenic stimulation, but each at different rates, although aryl sulphatase was unaffected. Such differences may be of importance when lymphocytes are used for diagnosis of inherited lysosomal deficiency diseases.
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PMID:Effects of mitogenic stimulation of lymphocytes on lysosomal enzyme activity. 643 92

Several lysosomal glycosidase activities were examined in vitro during heat-induced germination of Dictyostelium discoideum spores and were found not to be coordinately controlled. The level of beta-glucosidase activity increased significantly during the emergence stage of germination. Both alpha-glucosidase and N-acetyl-beta-glucosaminidase activities remained relatively constant until postemergence, when they increased slightly; alpha-mannosidase activity decreased during all stages of germination. The activity of beta-galactosidase increased slightly during spore swelling, fell below the level initially found in spores at zero time, and increased slightly during postemergence. The expression of all of these enzyme activities, except the increase in beta-galactosidase, appeared to require protein synthesis. Spores in the lag phase of germination which were exposed to severe environmental stress were deactivated and exhibited reduced levels of alpha-glucosidase, beta-glucosidase, and N-acetyl-beta-glucosaminidase activities. Prolonged heat activation treatment reduced the levels of lysosomal glycosidase activities in postactivated spores but did not change the subsequent enzyme patterns during the spore-swelling and emergence stages of germination.
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PMID:Expression of glycosidase activities during germination of Dictyostelium discoideum spores. 676 80

Leukocytes were isolated from 14 patients (7 males and 7 females ) with Gaucher disease of the Norrbottnian type (Type 3), 32 obligate heterozygotes (16 males and 16 females) for this disease and 20 controls (10 males and 10 females). After collection, the cells were transported in dry ice to the laboratory, where they were assayed. The assays were repeated after the cells had been stored for 12 months. beta-Glucosidase activity was assayed with D-[glucose-U-14C]glucosylceramide at pH 5.8 with Cutscum-Na-cholate as a detergent and 4-methylumbelliferyl-beta-glucoside at pH 4.1 with Triton-Na-taurocholate as a detergent. The activities of two marker enzymes, 4-methylumbelliferyl-beta-galactosidase and N-acetyl-beta-glucosaminidase, were assayed in aliquots of the same leukocyte samples. The activity of beta-galactosidase remained constant during storage, N-acetyl-beta-glucosaminidase increased, while beta-glucosidase decreased as assayed with the natural as well as with the artificial substrate. beta-Glucosidase activity was significantly lower in the female than in male controls and heterozygotes. When assayed with natural substrate beta-glucosidase activity in leukocytes from the male patients was 6--12% of the control mean value and 10--15% in those from the female patients. The corresponding figures found when the artificial substrate was used were 15--30% and 22--45%. The values for the heterozygotes were respectively 42--68% and 34--79% with the natural substrate, and 33--82% and 51--109% with the artificial substrate. No correlation was found between the age of the patient and the beta-glucosidase activity.
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PMID:Assay of the beta-glucosidase activity with natural labelled and artificial substrates in leukocytes from homozygotes and heterozygotes with the Norrbottnian type (Type 3) of Gaucher disease. 677 5

Fibroblasts from 13 homozygotes and 27 obligate heterozygotes with the Norrbottnian type of Gaucher disease and 17 controls were cultivated and assayed with five beta-glucosidase methods, two with D-[glucose-U-14C] glucosylceramide and three with the artificial substrate 4-methylumbelliferyl-beta-glucoside. Two marker enzymes were assayed on the same cell samples, 4-methylumbelliferyl-beta-galactosidase and N-acetyl-beta-glucosaminidase. The beta-glucosidase activity of cultured fibroblasts, as measured with all five beta-glucosidase methods, was significantly lower (P < 0.001) for Gaucher homozygotes than heterozygotes. There was no overlap between fibroblasts from Gaucher homozygotes and the others with any of the beta-glucosidase methods used. The beta-glucosidase activity was also significantly lower (P < 0.001) for Gaucher heterozygotes than controls. However, none of the five beta-glucosidase assays differentiated between all Gaucher heterozygotes and controls, as several overlaps occurred in each assay.
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PMID:Assay of the beta-glucosidase activity with natural labelled and artificial substrates in cultivated skin fibroblasts from homozygotes and heterozygotes with the Norrbottnian type of Gaucher disease. 677 99

Sixteen pregnancies at risk for Gaucher disease -- six with the Norrbottnian form, one with a juvenile form with a similar clinical course to the patients from Norrbotten and nine with the infantile from -- have been monitored by the assay of beta-glucosidase activity in cultivated amniotic fluid cells with natural labelled glycosylceramide as substrate. Two methods of cultivation were compared in respect of their effect on the activity of lysosomal enzymes. No significant difference was found between the two marker enzymes, beta-galactosidase and N-acetyl-beta-glucosaminidase, but the beta-glucosidase activity was significantly higher in the cells cultivated with one of the methods. In four of the pregnancies at risk, the beta-glucosidase activity in the cultivated amniotic fluid cells was less than 5% of that in the two control materials. These fetuses were regarded as affected with Gaucher disease and were aborted. Differentiation between controls and Gaucher heterozygotes was not possible in cultivated amniotic fluid cells. The diagnosis of Gaucher disease in the amniotic fluid cells was confirmed in three of the four cases by the assay of the beta-glucosidase activity in the liver nd brain of the aborted fetuses. The glucosylceramide content of the liver from two aborted fetuses was not augmented. The beta-glucosidase activity was examined in seven placentas from pregnancies at risk for Gaucher disease and found to be in agreement with that in the cultivated amniotic fluid cells.
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PMID:Prenatal diagnosis of Gaucher disease. Assay of the beta-glucosidase activity in amniotic fluid cells cultivated in two laboratories with different cultivation conditions. 678 Feb 54

Several glycosidase activities were measured in frontal gray matter of 4 brains from subjects affected by Creutzfeldt-Jakob disease. The changes of N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucosidase, alpha-fucosidase and alpha-mannosidase were not statistically significant but significant increases of beta-glucuronidase and beta-galactosidase activities were found. These results are in accordance with several reports on brain glycosidases in scrapie and Semliki Forest virus-infected brain and could explain some changes in brain glycoconjugate content previously observed in human and experimental Creutzfeldt-Jakob disease.
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PMID:Brain glycosidases in Creutzfeldt-Jakob disease. 678 37

An enzymatic profile of 20 strains of Pseudomonas maltophilia was undertaken with conventional plate tests, API ZYM, and 4-methylumbelliferyl-conjugated substrates. All strains produced DNase, RNase, arbutinase, esterases and lipases, mucinase, acid and alkaline phosphatases, alkaline pyrophosphate diesterase, phosphoamidase, beta-glucosidase, leucine arylamidase, and acetatase and were hemolytic for horse, sheep, and rabbit blood. The majority of strains produced chitinase, hyaluronidase, albuminase, valine arylamidase, trypsin, alpha- and beta-glucosidases, and N-acetyl-beta-glucosaminidase. API ZYM and 4-methylumbelliferyl-conjugated substrate assays are rapid, simple, specific, and sensitive and may be useful as diagnostic aids in the identification of P. maltophilia and other pseudomonads.
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PMID:Enzymatic profile of Pseudomonas maltophilia. 681 50

To study the role of lysosomal enzymes in glomeruli, we examined specific activities of lysosomal hydrolases in isolated glomeruli and, for comparison in isolated tubules, from rat kidney cortex of normal animals and animals with puromycin aminonucleoside nephrosis (PAN). Nephrotic syndrome was induced in rats by a single intraperitoneal injection of aminonucleoside and the rats were sacrificed at the time of peak proteinuria. Colloidal iron staining of renal cortex demonstrated decreased staining for the epithelial polyanion in animals with PAN. Lysosomal enzymes were determined by fluorogenic and colorimetric methods. In normal kidney, total specific activities of cathepsin beta 1, beta-2-fucosidase, acetyl-beta-glucosaminidase, and arylsulfatase were lower in glomeruli compared with tubules and with tissue slices of the same kidney. Total activity of acid phosphatase was higher in glomeruli than tubules. In glomeruli of PAN rats, there were lower activities of N-acetyl-beta-glucosaminidase, D-fucosidase, beta-glucosidase, beta-glucoronidase, and arylsulfatase compared with control rats. Activity of acid phosphatase, on the other hand, was higher in glomeruli of PAN than control rats. All differences were statistically significant. These studies demonstrate that (1) activities of lysosomal enzymes in normal glomeruli and in glomeruli of nephrotic rats have a property distinct from the rest of the kidney, and (2) the specific activities of lysosomal hydrolases are altered in glomeruli of rats with PAN. These studies suggest that changes in activities of lysosomal enzymes may be related to pathogenesis of this glomerulopathy.
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PMID:Activities of lysosomal enzymes in isolated glomeruli. Alterations in experimental nephrosis. 732 25


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