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)

Twenty four hour urine samples of male control and streptozotocin-diabetic Wistar rats were analysed for a series of commonly known kidney-specific enzymes, for electrolytes, creatinine, glucose, total protein and urine volume. The examination was done during two periods of 5 days between the 25th and 30th and the 32nd and 36th day after streptozotocin application. In the first period the animals had free access to food and water, whereas in the second period on days 32, 34 and 36 food was withdrawn. In the first observation period the diabetic rats showed increased excretion rates of 15 measured urinary parameters, while alanine aminopeptidase (EC 3.4.1.2) and gamma-glutamyltransferase (EC 2.3.2.2) activities were lowered and inorganic phosphate was unchanged. The removal of food resulted in decreased excretion values for alanine aminopeptidase, gamma-glutamyltransferase and total protein as compared with fasted nondiabetic animals. The activities of N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30), acid phosphatase (EC 3.1.3.2), lactate dehydrogenase (EC 1.1.1.27), pyruvate kinase (EC 2.7.1.40), C1-fructose 1.6-diphosphatase (EC 3.1.3.11) and the excretion values for sodium, calcium, magnesium, chloride and glucose were higher than in fasted nondiabetic rats. beta-Glucosidase (EC 3.2.1.21), potassium, inorganic phosphate, creatinine, and urine volume showed no differences between fasted diabetic and fasted control animals. The enzymes in the renal cortex at the end of the experiment showed only decreased activity of alanine aminopeptidase in diabetic rats. Lactate dehydrogenase, pyruvate kinase, beta-glucosidase, C1-fructose 1.6-diphosphatase and glucose 6-phosphatase (EC 3.1.3.9) were increased and gamma-glutamyltransferase, N-acetyl-beta-D-glucosaminidase, acid phosphatase and glucose 6-phosphate dehydrogenase (EC 1.1.1.49) showed no change.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Enzymuria in streptozotocin-diabetic rats. 353 86

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 contents of hexoses and hexosamines in brain, liver, and kidney of streptozotocin diabetic mice are significantly increased in comparison to the controls. These differences for hexoses contents in the heart are not significant. N-acetyl-beta-D-glucosaminidase and beta-D-glucosidase activities in brain, liver and kidney of diabetic mice are significantly higher when compared to the controls. However, beta-D-galactosidase activity is significantly lower in brain, liver, spleen and kidney of the diabetic mice, in comparison to the controls and similar in heart. alpha-D-Mannosidase activity of diabetic mice is significantly increased in spleen and heart and significantly decreased in liver and kidney. alpha-L-Fucosidase of diabetic mice shows higher activities, with significant differences, in liver and spleen; however, in heart and kidney the activities are significantly lower. Brain sialyltransferase and galactosyltransferase activities are significantly increased in diabetic mice; but for heart and kidney these differences are not significant. The activity for brain and kidney fucosyltransferase is not significant and that for the other assayed organs is significantly higher in comparison to the controls.
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PMID:Carbohydrate contents, and glycosidase and glycosyl transferase activities in tissues from streptozotocin diabetic mice. 392 73

The urinary excretion of N-acetyl-beta-D-glucosaminidase (NAG), beta-galactosidase (GAL), beta-glucosidase (GLU), and alkaline phosphatase (AP) was studied in 83 patients with renal allografts. Thirty of these patients had stable graft function and their urinary enzyme levels provided a range of normal values. Urinary lactic dehydrogenase (LDH) was estimated in 29 normal subjects and in 11 patients with renal allografts. Serum values for the five enzymes were also obtained. Urinary NAG excretion was abnormally high in 16 out of 17 (94%) episodes of acute rejection. The other urinary enzymes were raised less frequently. In nine patients studied before the onset of rejection urinary NAG activity rose up to three weeks before changes in other tests of renal function. Serum enzyme levels were not found to be of value in the diagnosis of rejection.
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PMID:Early warning of rejection? 457 44

Activities of certain acid hydrolases (viz. acid phosphatase, beta-glucosidase, beta-galactosidase, N-acetyl-beta-D-glucosaminidase and cathepsine) of post mitochondrial fraction of liver and spleen were studied during the course of Dipetalonema viteae infection in Mastomys natalensis. The values are significantly higher from prepatent to patent phase of infection as compared with normal animals. However, a decrease in the activity of hepatic acid phosphatase and N-acetyl-beta-D-glucosaminidase was noticed in latent phase of infection while a several fold increase in the activity of these enzymes was observed in splenic tissue when there were no detectable microfilariae (mf) in peripheral circulation. The results suggest that lysosomal acid hydrolases which constitute an important component of resistance may be activated by mf products through the sensitized cells of RE system.
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PMID:Lysosomal enzyme in Mastomys natalensis during Dipetalonema viteae infection. 641 75

Fluorescent Pseudomonas species (P. aeruginosa, P. fluorescens, P. putida) were tested for the presence of glycosidase activities (alpha-D-glucosidase, beta-D-glucosidase, alpha-D-galactosidase, beta-D-galactosidase, beta-xylosidase, alpha-D-mannosidase, alpha-L-fucosidase, beta-L-fucosidase, beta-D-glucuronidase and N-acetyl-beta-D-glucosaminidase). Some of the investigated glycosidases were always absent, while N-acetyl-beta-D-glucosaminidase was constantly present in all strains; 3 glycosidase activities were observed in association or separately. Serotype O11 of P. aeruginosa was found to be homogeneous with respect to some of those enzymatic activities. Search for beta-D-galactosidase, alpha-D-glucosidase and beta-D-glucosidase may be of diagnostic value in epidemiologic studies of P. aeruginosa.
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PMID:[Detection of glycosidases in Pseudomonas of the fluorescent group: relation between serotype and glycosidase activities in P. aeruginosa]. 642 62

The authors performed a comparative biochemical study of some enzymes of lysosomic origin (hyaluronidase, N-acetyl-beta-D-glucosaminidase, beta-glucosidase, beta-galatosidase and acid phosphatase), of the state of enzyme substrate system N-acetylneuraminic acid---aldolase of neuramic acid and of the activity of lactatedehydrogenase (soluble in cytosol and bound on mitochodria) in the liver, lungs and blood serum of rats at various regimens of the inhalation action of CCl4. On the basis of results obtained they determined the biological importance of the change of activity of enzymes differently localized in cells at the adaptation of an organisme to the noxious action of CCl4.
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PMID:The influence of tetrachloromethane on subcellular structures of rat hepatocyte lysosomal and cytoplasmic enzymes of the liver, lungs and blood serum of rats during continuous and intermittent action of tetrachloromethane. 719 Sep 85

Members of the Streptococcus sanguis group (SSG) and Streptococcus milleri group (SMG) were screened for their ability to produce glycosidase, arylamidase (peptidase), protease, dextranase and glycosyltransferase activities. Species within each group produced unique patterns of activity. The most commonly produced glycosidases were beta-D-glucosidase, beta-D-galactosidase, N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase and the least commonly produced glycosidase activity was beta-fucosidase with Streptococcus intermedius (SMG) being the only species capable of producing the activity. For arylamidase activity, the most commonly produced type was lysine-arylamidase. Glycosidase and arylamidase activities were localized to particular sub-cellular fractions. alpha-galactosidase was found only in culture supernatant fluids whereas N-acetyl-beta-D-glucosaminidase was found in all fractions; the culture supernatant, cell wall, cell membrane and cytoplasm. No arylamidase activity was seen in culture supernatants. Phe-arg-arylamidase was found only in cytoplasmic fractions whereas val-pro-argarylamidase was found in cell walls, cell membranes and cytoplasmic fraction. Protease activity was measured as the degradation of bovine serum albumin (BSA) and casein. Casein was degraded by a number of strains whereas no species/strains were able to degrade BSA. Streptococcus intermedius, Streptococcus constellatus (SMG), Streptococcus mitior and Streptococcus defectivus (SSG) were the only species that produced hyaluronidase and no species produced chondroitin sulphatase. The groups were also examined for their abilities to produce glycosyltransferase and dextranase. Strep. sanguis, Streptococcus gordonii, Streptococcus mitis and Streptococcus oralis produced glucosyltransferase and, with the exception of the latter species, fructosyltransferase. No species within the SMG was capable of producing either glycosyltransferase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Degradative enzymes of oral streptococci. 778 31

The expression of some faecal hydrolytic enzymes in rats fed for 4 months on sucrose or starch enriched diets was compared with a standard diet. The assay reliability was confirmed for animal and experimental variability. The beta-D-glucuronidase and beta-D-glucosidase activities were always higher in rats fed on starch than on other diets. N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase showed decreased activity when passing from a standard to a sucrose, and from a sucrose to a starch diet. There was little modification in the levels of faecal alpha-D-glucosidase, sulphatase and protease with the various experimental diets.
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PMID:Carbohydrate enriched diets and bacterial glycosidases in rat faeces. 830 95

Different surveys have been carried out on the plasma activities of different glycosidases in patients with insulin-dependent diabetes mellitus, but research on urinary glycosidases in this disease is scanty and incomplete. To elucidate the behavior of these lysosomal enzymes in the metabolic alterations occurring in the glomerular basal membrane during the initial stages of diabetic nephropathy, we conducted a prospective study to examine the urinary activities of N-acetyl-beta-D-glucosaminidase (NAG), alpha-D-mannosidase, alpha- and beta-D-glucosidase, alpha-L- and beta-D-fucosidase, and beta-D-galactosidase in patients with type I insulin-dependent diabetes mellitus, surveyed over 18 months, whose early diabetic nephropathy was detected by the presence of microalbuminuria. The simultaneous determination of beta 2-microglobulin in urine confirmed the glomerular origin of the albuminuria. No statistically significant correlation was found between the levels of albuminuria and the activities of any of the glycosidases analyzed. In the diabetic patients, a significant decrease was observed in the activities of all the enzymes (p < 0.05), except NAG and alpha-D-mannosidase, although the decrease in the latter was very close to statistical significance (p = 0.028, unilateral; p = 0.057 bilateral). Similarly, in the patients, there was a significant negative correlation (p < 0.05) with the serum levels of fructosamine, except with beta-D-galactosidase, which showed a positive correlation (p < 0.05) with fructosamine and blood HbA1c.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Prospective study of the enzymatic activities in urine of N-acetyl-beta-D-glucosaminidase, alpha-D-mannosidase, alpha- and beta-D-glucosidases, alpha-L- and beta-D-fucosidases, and beta-D-galactosidase in type I diabetes mellitus with early nephropathy. 834 14


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