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)

Systemic release of lysosomal enzymes and local release in the pulmonary microcirculation from sequestrated and activated leucocytes could be an important factor in the development of the lung microvascular injury seen after septicaemia. The maximal activities of 11 lysosomal acid hydrolases (acid phosphatase, alpha- and beta-glucosidase, alpha- and beta-galactosidase, alpha-mannosidase, beta-acetylglucosaminidase, beta-glucuronidase, arylamidase and cathepsins B and C) were measured in serum and lung lymph from seven sheep before and after infusion of live E. coli bacteria. In the early phase of septicaemia (the first hour) the activities of eight enzymes were increased in serum and/or lung lymph (1.1 to 2X pre-infusion values). In the late phase, 3-4 h after sepsis, there were significantly elevated serum activities of beta-glucosidase (5.4X), alpha- and beta-galactosidases (2.7X, 1.5X), beta-acetylglucosaminidase (2.0X) arylamidase (1.2X) and cathespin B (1.7X). In lymph acid phosphatase (1.7X), alpha- and beta-glucosidases (1.6X, 6.4X), alpha- and beta-galactosidases (2.1X, 1.7X). Beta-acetylglucosaminidase (2.6X), and beta-glucuronidase (4.0X pre-infusion) were elevated. The findings of a heterogenicity of changes in serum and lymph activities, as well as the large molecular sizes of some of the enzymes with changed activities indicated to us that permeability changes were not major causes of increased lymph enzyme activities. The results could indicate a local release of enzymes either from sequestrated leucocytes or lung tissue due to local reactions in the lung or lung microvessels. The heterogenous changes in activities for the various lysosomal enzymes as found in the present study indicated that measurement of only one enzyme could be misleading.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Lysosomal enzyme pattern in lung lymph and blood during E. coli sepsis in sheep. 329 74

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

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

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

An antigen fraction from Faenia rectivirgula (Micropolyspora faeni) having diagnostic significance for farmer's lung disease was isolated by Sephadex G-200 and G-100 fractionations. Antibody raised against this antigen fraction was used to make an immunoaffinity column to purify crude culture filtrate antigens of F. rectivirgula. The antigen has a molecular weight of 66,000 and an isoelectric point between pH 6.0 and 6.5. The yield of this antigen fraction was 1.02% of the total protein of the crude antigen. Although the crude antigen showed activity for several enzymes, the purified antigen showed enhanced activity for acid phosphatase and beta-glucosidase. Using this antigen fraction, an ELISA was developed for detecting circulating specific IgG antibody in farmer's lung patients. The antigen can be standardized by its immunochemical characteristics and may be used to detect circulating antibodies in the sera of patients with dependability and reproducibility.
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PMID:A partially purified antigen from Faenia rectivirgula in the diagnosis of farmer's lung disease. 358 71

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

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

In primary astrocyte cultures beta-glucosidase (EC 3.2.1.21) and beta-galactosidase (EC 3.2.1.23) showed pH optima and Km values identical to rat brain enzymes, using methylumbelliferyl glycosides and labeled gluco- and galactocerebrosides as substrates. The activities of both glycosidases increased in culture up to 3-4 weeks. In rat brain only galactosidase increased; glucosidase activity declined between 12-20 days after birth. The specific activities were two- to sixfold higher in astrocyte cultures than in rat brain. These activities were not due to uptake of enzymes from the growth medium. Secretion of beta-galactosidase, but not beta-glucosidase nor acid phosphatase could be demonstrated. These results support the suggestion of a degradative function for astrocytes in the brain.
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PMID:beta-Glucosidase and beta-galactosidase in primary cultures of rat astrocytes: comparison to the brain enzymes. 391 92

Evidence has been found for a generalized change in the post-translational modification of lysosomal enzymes during development of Dictyostelium discoideum. The physical and antigenic properties of four developmentally regulated lysosomal enzymes, N-acetylglucosaminidase, beta-glucosidase, alpha-mannosidase, and acid phosphatase, have been examined throughout the life cycle. In vegetative cells, a single major isoelectric species is detected for each enzymatic activity on native nonequilibrium isoelectric focusing gels. Between 6 and 10 hr of development, all activities, including the preformed enzyme, become less negatively charged, resulting in a modest but reproducible shift in the isoelectric focusing pattern. This alteration is not detected by native gel electrophoresis at constant pH. As development continues, the specific activity of beta-glucosidase, alpha-mannosidase, and acid phosphatase continues to increase and coincidentally, new, less acidic isozymic bands of activity can be observed on both gel systems. Some of these new isozymes accumulate preferentially in anterior cells, while others accumulate preferentially in posterior cells of migrating slugs. N-Acetylglucosaminidase does not increase in specific activity late in development and no new isozymic species appear. Using a monoclonal antibody that reacts with sulfated N-linked oligosaccharides shared by vegetative lysosomal enzymes in D. discoideum, the antigenicity of the developmental isozymes has been characterized. All of the enzymatic activity present during vegetative growth and early development is immunoprecipitable. However, the less negatively charged isozymes that accumulate after aggregation are not recognized by the antibody. Nonantigenic acid phosphatase and alpha-mannosidase are found in both anterior and posterior cells from migrating pseudoplasmodia. Since each enzyme is coded by a single structural gene, these results suggest that the isozymes present late in development arise from the synthesis of the same polypeptides with altered post-translational modifications. The appearance of anterior and posterior specific isozymes is likely to be the result of cell type specific changes in the glycoprotein modification pathway for newly synthesized proteins.
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PMID:Developmental changes in the modification of lysosomal enzymes in Dictyostelium discoideum. 391 96

Activity of lysosome enzymes (acidic phosphatase, beta-glucosidase, DNAase, RNAase and cathepsin D) is determined for its variation in different organs of rainbow trout during complete fasting. It is shown that the activity of most enzymes of concern almost in all organs except skeletal muscles is on the higher level in trouts fasted for 30 days than in the control ones. With an increase of the fasting term to 60 days the acid phosphatase, DNAase, RNAase activity decreases while the glucosidase and cathepsin D activity in some organs increases. Variations detected in the enzyme profile of the trout lysosomes under fasting are of adaptive character.
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PMID:[Changes in the activity of trout lysosomal enzymes during fasting]. 392 43


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