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)

API ZYM and API An-Ident enzymatic substrate tests were done on six oral species which are difficult to characterize with conventional biochemical tests. "Bacteroides forsythus, the "fusiform" Bacteroides species (A. C. R. Tanner, M. A. Listgarten, M. N. Strzempko, and J. L. Ebersole, manuscript in preparation), is difficult to cultivate in broth media, yet it gave 15 positive tests in these series. The tests were able to separate this new species from species of Capnocytophaga and Fusobacterium. "B. forsythus" reactions were similar but not identical to those of reference Bacteroides species. Positive reactions for alpha-glucosidase, beta-glucosidase, alpha-fucosidase, and alpha-glucuronidase suggest that "B. forsythus" may be saccharolytic. It was the only species tested which was trypsin positive. Wolinella species, Campylobacter concisus, B. gracilis, and Eikenella corrodens are asaccharolytic, and characterization relies heavily on sensitivities to inhibitory agents. These species reacted weakly in the API ZYM and API An-Ident enzymatic substrate tests, and the reactions were not useful for separating these species. The enzyme reactions differentiated Wolinella recta and C. concisus from Selenomonas sputigena, another oral motile but saccharolytic organism.
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PMID:API ZYM and API An-Ident reactions of fastidious oral gram-negative species. 393 May 58

With several isolates of T. aquaticus rotund bodies (rbs) have been artificially induced. The most active agents were lysozyme, pronase (not trypsin), cellulase (not alpha-amylase or beta-glucosidase), penicillin and some mineral salts. Two modifications of rbs were observed: the vesticular type arising from single cells or filaments and the aggregate-rbs resulting from secondary associations of several cells or filaments. In both cases the primary event is a partial detachment of the outer layer of cell envelopes followed by its swelling to form a hyaline bleb. Within these osmotically stable blebs cells and/or filaments involved in the ribs production become irreversibly trapped. Appearance of filaments and rbs in stationary phase cultures are discussed as a consequence of unbalanced growth culminating in abnormal autolytic reactions.
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PMID:[Experimental induction of rotund bodies in Thermus equaticus]. 615 8

Certain properties of experimental pellicles formed by the adsorption of salivary components on hydroxyapatite surfaces change over time. To determine whether enzymes likely to be present in the oral environment could induce such changes, pellicles were treated with saliva which had been incubated for 18 h at 35 degrees C to promote the elaboration of microbial enzymes. This treatment markedly reduced the numbers of Streptococcus mutans MT3 and JBP and S. sanguis FC-1 and C5 cells which attached, but it had little or no effect on the attachment of S. mitis RE7, Actinomyces viscosus LY7 and CK-8, Bacteroides gingivalis 381, or B. melaninogenicus subsp. intermedius 581. Heating the incubated saliva at 60 degrees C for 30 min partially reduced its pellicle-modifying activity, whereas heating at 80 degrees C for 30 min or 100 degrees C for 15 min completely eliminated such activity. This indicated that the saliva contained heat-labile substances, presumably enzymes, which could affect the pellicle receptors involved in the attachment of S. mutans and S. sanguis. Treatment of saliva-treated hydroxyapatite with commercially obtained enzyme preparations also affected bacterial attachment. Thus, treatment with galactose oxidase reduced the numbers of the S. mutans strains which attached, whereas treatment with neuraminidase reduced the adsorption of S. sanguis FC-1 but not that of S. sanguis C5. Treatment with beta-glucosidase preparations derived from almonds significantly reduced the attachment of all of the streptococcal strains studied, but, when subjected to isoelectric fractionation, the adherence-inhibiting activity did not correlate directly with beta-glucosidase activity. Treatment of the pellicles with trypsin or eight other glycosidases did not affect streptococcal attachment. Exposure of the enzymatically modified pellicles to fresh saliva did not restore the streptococcal receptors. Collectively, the data suggest that some bacterial receptors in the pellicle coating of teeth can be modified by enzymes likely to be present in the oral environment, and these interactions may affect oral bacterial ecology.
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PMID:Enzymatic modification of bacterial receptors on saliva-treated hydroxyapatite surfaces. 628 Nov 93

The H-2Kk glycoprotein has been isolated by monoclonal antibody affinity chromatography, and an analysis of the asparagine-linked oligosaccharides present at the two major glycosylation sites has been performed. Antigen obtained from the AKTB-1b B-cell lymphoma that had been labeled with [2,6-3H]mannose for 5 or 21 h or for 5 h followed by a 5-h chase was digested exhaustively with trypsin. Each glycosylation site was then isolated by reverse phase high performance liquid chromatography using a C18 column. After removal from the peptide backbone by the almond emulsin peptide: N-glycosidase, the oligosaccharides from each isolated site were analyzed by gel filtration, ion exchange chromatography, concanavalin A affinity chromatography, and glycosidase treatment to assess the contribution of sialic acid and branching patterns of the oligosaccharide backbones to the overall microheterogeneity. The glycosylation of the H-2Kk antigen derived from several different AKTB-1b tumor preparations was examined during a period covering 1 year, during which time the tumor was passaged continuously in vivo in 2-week cycles. Our results conclusively demonstrate that the pattern of oligosaccharide microheterogeneity at the two glycosylation sites of the H-2Kk antigen derived from AKTB-1b cells is stable and that each site differs as to the specific array of oligosaccharide types found on the fully processed glycoprotein. In addition, this report describes an analytical scheme employing reverse phase high performance liquid chromatography to follow oligosaccharide processing and hydrolysis of the N-glycosidic bond by the peptide: N-glycosidase.
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PMID:Stable oligosaccharide microheterogeneity at individual glycosylation sites of a murine major histocompatibility antigen derived from a B-cell lymphoma. 660 28

A radioactive glycopeptide with a molecular weight of 13 200 was isolated from beta-glucosidase A3 after labeling the active site with [3H]conduritol B epoxide and cleavage with trypsin. The glycopeptide consists of 63 amino acids and 29 +/- 1 sugar residues. Its amino acid sequence was derived from the results of sequence analysis of peptic and cyanogen bromide peptides. The radioactive inhibitor is bound to aspartic acid 12 of the sequence, the sugar residues are probably bound as N-glycosides to asparagine 48 and asparagine 56, since O-glycosidic linkages have been ruled out.
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PMID:Isolation and structure of a tryptic glycopeptide from the active site of beta-glucosidase A3 from Aspergillus wentii. 678 81

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

Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase, alpha-galactosidase, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase, trypsin, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
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PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46

Amylase, alpha- and beta-glucosidase, alpha- and beta-galactosidase, beta-fructosidase, trypsin, aminotripeptidase, leucine-aminopeptidase, prolinase, prolidase glycyl-L-leucine dipeptidase and glygylglycine dipeptidase are present in the 3rd instar larvae of Chilo auricilius.
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PMID:Digestive enzymes in the gut and salivary gland of the larvae of Chilo auricilius Ddgn. 698 21

When cells of the slime mould Dictyostelium discoideum are allowed to starve in the presence of alpha-chymotrypsin, they are blocked in development at the stage where tight aggregates form tips. Analysis of developmentally regulated enzymes has shown that alpha-mannosidase, beta-N-acetylglucosaminidase, threonine deaminase, tyrosine aminotransferase, beta-glucosidase and the carbohydrate-binding protein discoidin are unaffected, but enzymes that show an increase in specific activity during post-aggregative development, namely glycogen phosphorylase, UDP-glucose pyrophosphorylase, UDP-galactose 4-epimerase, UDP-galactose polysaccharide transferase and alkaline phosphatase, did not show the characteristic increase when development was blocked by alpha-chymotrypsin. Recovery of cells from the effects of alpha-chymotrypsin was accompanied by the formation of fruiting bodies and a concomitant increase in the specific activity of UDP-glucose pyrophosphorylase. Uptake or efflux of 45Ca2+ was not altered in the presence of alpha-chymotrypsin. Cells allowed to develop in alpha-chymotrypsin, or treated with the enzyme for 15 min, had a markedly reduced ability to bind cyclic AMP with low affinity; high-affinity binding was unaffected. Pronase had a similar effect on cyclic AMP binding, but trypsin, which does not alter developmental processes, has no effect on cyclic AMP binding to D. discoideum cells.
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PMID:Developmentally regulated enzymes and cyclic AMP-binding sites in Dictyostelium discoideum cells blocked during development by alpha-chymotrypsin. 715 Feb 39

By using a suckling mouse assay, heat-stable enterotoxin (ST) was purified from the culture filtrate of Yersinia enterocolitica isolated from a diarrheal patient. The purification procedures involve ultrafiltration with an Amicon HIP-10 hollow fiber, ethanol fractionation, protamine sulfate treatment, diethylaminoethyl-Sephacel and hydroxylapatite column chromatographies, and Sephacryl S-200 superfine gel filtration. About 408-fold purification was achieved, with a yield of 12.0%. The minimal effective dose of purified ST was about 110 ng in the suckling mouse assay. The molecular weight of purified ST was 9,000 by Sephadex G-100 superfine gel filtration. The purified ST was stable to heating (100 degrees C for 20 min, 121 degrees C for 20 min) and did not lose its toxicity after treatment with protease, trypsin, lipase, phospholipase C, ribonuclease, deoxyribonuclease, beta-glucosidase, and neuraminidase. The purified ST was separated by isoelectric focusing into two active fractions, with pI's of 3.29 (ST-1) and 3.00 (ST-2), respectively. Antiserum from guinea pigs immunized with the purified ST neutralized the activity of both Y. enterocolitica ST and Escherichia coli ST.
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PMID:Partial purification and characterization of heat-stable enterotoxin produced by Yersinia enterocolitica. 721 60


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