Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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 enzymatic activities of 53 strains of Pseudomonas cepacia were determined by using the API ZYM system. Strong alkaline phosphatase, acid phosphatase, butyrate esterase, caprylate esterase, myristate lipase, leucine arylamidase, and phosphoamidase activities were consistently detected in all strains. Weak activities were observed for valine arylamidase, beta-glucosidase, and N-acetyl-beta-glucosaminidase. No activities could be demonstrated for cystine arylamidase, trypsin, chymotrypsin, alpha-galactosidase, beta-galactosidase, beta-glucuronidase, alpha-glucosidase, alpha-mannosidase, and alpha-fucosidase. Enzymatic activities of pseudomonads may provide useful information about their pathogenesis and information for identification of Pseudomonas species.
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PMID:Enzymatic characterization of Pseudomonas cepacia by API ZYM profile. 335 98

Nineteen hydrolytic enzymes were detected in individual adult Pergamasus longicornis (Berlese) mites--amylase, hide protease, alkali phosphatase, esterase (C4), esterase lipase (C8), lipase (C14), leucine arylamidase, valine arylamidase, cystine arylamidase, acid phosphatase, phosphoamidase, alpha-galactosidase, beta-galactosidase, beta-glucuronidase, alpha-glucosidase, beta-glucosidase, N-acetyl-beta-glucosaminidase, alpha-mannosidase, and alpha-fucosidase. All but the phosphatases were detected for the first time. Tryptic and chymotryptic activity were consistently not demonstrable. Comparisons are made with saprophagous mites. No clear enzymic specialization for predation was found.
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PMID:Digestion in the soil predatory mite Pergamasus longicornis (Berlese) (Acari: Mesostigmata: Parasitidae)--detectable hydrolases. 356 25

Platelets were isolated from blood donated by 57 diabetic subjects, 41 insulin-dependent and 16 non insulin-dependent, ranging in age from 19 to 78 years, and by 54 healthy non-diabetic subjects ranging from 19 to 63 years of age. The platelets were ruptured by sonication and resultant preparations assayed for their levels of activity of seven acid glycohydrolases. Platelets from diabetic subjects contained only 50% of the alpha-L-fucosidase activity and about 60% of the acid phosphatase, beta-D-galactosidase, and beta-D-glucosidase activities of platelets from non-diabetic individuals; the differences were statistically significant. N-acetyl-beta-D-glucosaminidase activity in platelets from diabetic subjects was reduced by about 15% from normal levels while beta-D-glucuronidase and alpha-D-mannosidase activities were similar to those from non-diabetic individuals. A comparison of the data from older insulin-dependent diabetic and normal subjects with a similar age distribution yielded identical results for the two groups in all enzymes tested except fucosidase. Platelets of non insulin-dependent diabetics and those from non-diabetic subjects of a similar age distribution appear to possess similar levels of these acid hydrolases. There was no difference in levels of these platelet acid hydrolases between males and females in either the diabetic or non-diabetic group. Within the diabetic group, there was no difference in these platelet acid hydrolase activities between subjects with retinopathy and without retinopathy. There was no correlation of the enzyme activity levels of platelets from diabetic subjects with concentration of glycosylated haemoglobin, serum triglycerides or serum cholesterol.
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PMID:Effect of diabetes mellitus on selected acid hydrolase activities in human platelets. 360 21

The taxonomic relationship of 116 isolates of Pasteurella haemolytica was re-investigated by conventional phenotypic characterization. Seventy-nine characters were examined. Ninety strains were classified with previously described biovars of P. haemolytica. The remaining strains made up at least six new biogroups within the P. haemolytica-complex. "Key-characters" separating these groups included ornithine, L(+)arabinose, D(-)sorbitol, cellobiose, beta-glucosidase, glycosides and alpha-fucosidase. The taxonomic significance of these characters is uncertain. Determinations of genome size, mol% G + C in DNA and DNA:DNA hybridizations are in progress to obtain further information on the taxonomic significance of the present findings.
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PMID:Re-investigations of selected bovine and ovine strains previously classified as Pasteurella haemolytica and description of some new taxa within the Pasteurella haemolytica-complex. 373 16

In human freshly prepared platelets the following lysosomal enzymes were studied: alpha-mannosidase, alpha-fucosidase, beta-galactosidase, beta-glucosidase, beta-glucuronidase, beta-N-acetylglucosaminidase and acid phosphatase. For each of the examined enzymes the conditions providing maximal activity (pH, buffer), kinetic parameters (saturating substrate concentration and Km) as well as heat stability were established. On the basis of these parameters it is suggested that many of the serum glycohydrolases may be platelet derived.
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PMID:Lysosomal enzymes in human platelets. 383 17

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

Some glycosidase activities have been determined in blood sera from 21 patients who ingested a toxic oil (rapeseed oil denatured with aniline(s) and treated by a thermal process). The samples were collected from the same patients on 3 or 4 occasions during a period of 11-12 mth. During this period, the clinical state of the patients improved and, generally, they were restored to health. beta-N-Acetylglucosaminidase, alpha-L-fucosidase, beta-D-glucuronidase, beta-D-glucosidase and alpha-D-mannosidase activities, which were higher in patients than in 17 controls during the first mth decreased to normal values in the period studied, 11-12 mth. In contrast, beta-D-galactosidase, alpha-D-galactosidase and alpha-D-glucosidase activities, which were initially lower in patients than in controls, were finally similar or higher than in controls. One explanation for these results could be the possible alteration of the cell membrane(s) by the toxic substance(s).
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PMID:Glycosidase activities in sera from convalescent patients who ingested a toxic oil. 398 46

The activities of six glycosidases in a rat colorectal adenocarcinoma were measured and compared with those of normal colonic mucosa. The specific activities of beta-galactosidase (EC 3.2.1.23) and beta-glucuronidase (EC 3.2.1.31) in the adenocarcinoma were similar to those of the corresponding ones in the normal mucosa, whereas those of beta-N-acetylglucosaminidase (EC 3.2.1.30), alpha-L-fucosidase (EC 3.2.1.51), alpha-galactosidase (EC 3.2.1.22) and beta-glucosidase (EC 3.2.1.21) were reduced in the former as compared with those in the latter. In the case of alpha-L-fucosidase, two forms were newly detected in the tumor. The relative abundance of three forms of beta-N-acetylglucosaminidase was quite different between the adenocarcinoma and the normal mucosa, and the level of the intermediate form in the tumor was markedly reduced. However, thermostability and Km values of two forms A and B in the tumor were not different from those of the corresponding ones in the normal tissue.
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PMID:Alteration in glycosidases from well-differentiated colorectal adenocarcinoma of rat. 404 71

The following enzymes of lysosomal origin were fluorimetrically determined in maternal plasma from the second to the ninth month of pregnancy at 1-mth intervals: beta-D-N-acetylglucosaminidase (EC 3.2.1.30), beta-D-glucuronidase (EC 3.2.1.31), beta-D-glucosidase (EC 3.2.1.21), beta-D-galactosidase (EC 3.2.1.22), alpha-D-galactosidase (EC 3.2.1.23), alpha-L-fucosidase (EC 3.2.1.51) and alpha-D-mannosidase (EC 3.2.1.24) (pH 4.0). As reference microsomal alpha-D-mannosidase (pH 5.7) was also studied. Thirty-eight healthy women, aged 18-37 yr, who had a normal pregnancy followed by normal parturition, were studied. All enzymes, with the only exception of beta-D-galactosidase, showed a progressive and statistically significant increase of activity throughout pregnancy. At the end of pregnancy, the increase ranged from a maximum of 5.6-fold for beta-D-N-acetylglucosaminidase to a minimum of 0.55-fold for alpha-D-mannosidase, pH 5.7. In the case of beta-D-N-acetylglucosaminidase, the level at the fifth month of pregnancy was significantly higher than that at the third month, and from the sixth to the ninth month each level significantly differed from that of the month immediately preceding.
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PMID:Behaviour of several enzymes of lysosomal origin in human plasma during pregnancy. 609 42

Coated vesicles from calf brain and rat liver contain cryptic receptors which recognize and bind lysosomal enzymes via mannose 6-phosphate residues on oligosaccharide side chains (Campbell, C. H., Fine, R. E., Squicciarini, J., and Rome, L. H. (1983) J. Biol. Chem. 258, 2628-2633). In addition to mannose 6-phosphate receptors, we now report that coated vesicles from calf brain and rat liver contain the lysosomal enzymes alpha-L-fucosidase, beta-galactosidase, beta-glucosidase, beta-hexosaminidase, alpha-L-iduronidase, and alpha-mannosidase. Enzyme activities co-migrated with coated vesicles purified by agarose gel electrophoresis. Treatment of intact coated vesicles with pronase (0.05 mg/ml) had little effect on lysosomal enzyme activities, whereas a similar treatment of coated vesicles in the presence of 0.045% taurodeoxycholate resulted in the loss of most of the enzyme activities. Addition of 10 mM mannose 6-phosphate to disrupted liver coated vesicles specifically displaced up to 80% of the cryptic lysosomal enzyme activity. Disrupted liver coated vesicles and highly purified liver lysosomes were treated with anti-beta-hexosaminidase A and anti-beta-galactosidase antibodies and immunoprecipitates were analyzed by polyacrylamide gel electrophoresis. High molecular weight bands were present in the coated vesicle immunoprecipitates which were not present in the lysosome immunoprecipitates. The data suggest that coated vesicles contain mannose 6-phosphate receptor-bound lysosomal enzymes, some of which are of a higher molecular weight form. These higher molecular weight forms may represent newly synthesized enzymes that are en route to lysosomes.
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PMID:Coated vesicles from rat liver and calf brain contain lysosomal enzymes bound to mannose 6-phosphate receptors. 613 57


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