Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. Six weeks after the injection of streptozotocin at 125 mg/kg i.p. in the AV line nondiabetic Chinese hamsters, the animals showed hyperglycemia, increased kidney, pancreas and stomach weights and stomach glucagon contents and depletion of insulin and glucagon in the pancreas. 2. Plasma beta-D-galactosidase and N-acetyl-beta-D-glucosaminidase were elevated; whereas alpha-D-glucosidase was decreased and alpha-D-galactosidase remained unchanged in the plasma. 3. In the kidney, streptozotocin-diabetes led to depression of alpha-D-mannosidase, beta-D-fucosidase and N-acetyl-beta-D-glucosaminidase activities in both 12,000 g supernatant and precipitate fractions, decreases in alpha-D-glucosidase in the supernatant only and no change in alpha-L-fucosidase, alpha-D-galactosidase, beta-D-galactosidase and beta-D-glucuronidase. 4. In the liver, significant increases in N-acetyl-beta-D-glucosaminidase, alpha-D-galactosidase, beta-D-galactosidase, beta-D-fucosidase, beta-D-glucosidase and alpha-D-mannosidase were found in either the supernatant or the precipitate fraction of the diabetic animals. The data indicate diabetes-dependent tissue-specific changes in glycohydrolases in the Chinese hamster.
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PMID:Alterations in glycohydrolase activities in streptozotocin-diabetic Chinese hamsters (Cricetulus griseus). 31 16

On the basis of experimental research results a method to assess the functional state of pulmonary alveolar macrophages in rabbits and rats has been proposed as a criterion of the biological effect of chemical atmospheric pollutants. The test involves a cytological assay, determination of the viable cells quantity and of the phagocytic competence, and also the biochemical study of alveolar macrophages enzymes activity (acid phosphatase, beta-glucuronidase, lysozyme, beta-galactosidase, beta-glucosidase, N-acetyl-beta-D-glucosaminidase). It has been shown that this method is informative and reliably reproducible, and that it was reasonable to use it in environmental health and other branches of experimental biology and medicine.
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PMID:[Method of studying the functional state of pulmonary alveolar macrophages during exposure to atmospheric pollutants]. 71 64

A number of adsorbents useful for purifying glycosidases were synthesized and their adsorption and characteristics were examined using partially purified glycosidase mixtures from Takadiastase or soybean. These adsorbents were prepared by coupling di-epsilon-aminocaproyl-p-aminophenyl N-acetyl-1-thio-beta-D-glucosaminide, beta-D-glucoside, beta-D-galactoside or alpha-D-mannoside with CNBr-activated Sepharose 4B. Many glycosidases were adsorbed on the four adsorbents at low ionic strength, and increase of the ionic strength caused the enzymes to be eluted. However, the specificity of the adsorbents, contrary to our expection, was very low. All of these adsorbents adsorbed Taka N-acetyl-beta-D-glucosaminidase [EC 3.2.1.30], Taka beta-D-glucosidase [EC 3.2.1.21], and Taka beta-D-galactosidase [EC 3.2.1.23] at low ionic strength. The order of elution of these three enzymes by a linear gradient of ionic strength was the same in the four adsorbents, the order being beta-D-galactosidase, beta-D-glucosidase, and N-acetyl-beta-D-glucosaminidase. Soybean glycosidases also showed nearly the same elution pattern, though the ionic strength of the eluate was slightly lower than with Taka glycosidases. Soybean alpha-D-mannosidase [EC 3.2.1.24] was also adsorbed on these adsorbents, and was eluted between beta-D-glucosidase and N-acetyl-beta-D-glucosaminidase. These adsorption phenomena were not specific as regards the structure of the glycoside moiety, but they were useful for purifying glycosidases, possessing good reproducibility with easy activation and mild operating conditions.
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PMID:Affinity chromatography of glycosidases. Preparation and properties of affinity column adsorbents. 94 2

Biochemical study of the activity of the enzyme systems of different localization in the cell connected with the subcellular structures - lysosomes (hyaluronidase, N-acetyl-beta-D-glucosaminidase, beta-glucosidase) and hyaloplasm-soluble (aldolase of neuraminic acid), and also a study of the state of the enzyme-substrate groups, belonging to the immunoreactive biopolymeres containing a carbohydrate (glucoproteins, glycosaminoglycanes) was carried out in the tissues of different organs (the liver, kidneys, small intestine, skin) and in the blood serum of albino rats exposed to the isolated and joint (in combination with various doses of ultraviolet irradiation) action of the chemical allergen (dinitrochlorbenzene). General and specific regularities of metabolic reactions, the appearance of which could presumably be connected with the development of delayed allergy were revealed.
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PMID:[Study of metabolic mechanisms of the isolated and combined effect of a chemical allergen]. 102 7

Variations of glycoprotein components such as hexose, hexosamine, and sialic acid and lysosomal glycosidases such as beta-D-glucosidase, beta-D-galactosidase, and N-acetyl-beta-D-glucosaminidase were studied in the tumor tissue from various stages of cervical carcinoma of the uterus. Carbohydrate components of glycoprotein were found to be markedly reduced, and the reduction was very much significant in hexosamine and sialic acid in the advanced stages. Lysosomal glycosidases exhibited a significant increase, and among them N-acetyl-beta-D-glucosaminidase exhibited a prominent increase, in the advanced stages of cervical carcinoma of the uterus.
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PMID:Studies on variations of glycoproteins and lysosomal hydrolases in human uterine cervical carcinoma. 144 83

The serum concentrations of FSH, LH, prolactin, testosterone, and estradiol and the enzymatic activities of hyaluronidase, glucosidases (alpha-glucosidase, beta-glucosidase, alpha-mannosidase, N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, and beta-galactosidase), lactate dehydrogenase and its isoenzymes (LDH1, LDH2, LDH3, LDH-X, LDH4), and total proteins were measured in the semen of 69 subjects (8 normozoospermic controls, 7 secretory, and 54 excretory azoospermic subjects). FSH levels rose with the deterioration in spermatogenesis and served to differentiate the secretory from the excretory azoospermias. The only source of hyaluronidase and LDH-X in the ejaculate is the spermatozoa. alpha-Glucosidase activity essentially originates in the epididymis. The seminal determination of alpha-glucosidase and, to a lesser extent, alpha-mannosidase and N-acetyl-beta-D-glucosaminidase helps rapidly, sensitivity, reliably, and noninvasively to differentiate secretory azoospermias (with higher enzymatic activity) from the excretory type (less enzymatic activity) and may be of use in identifying with a certain degree of reliability the site of obstruction in the male genital tract.
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PMID:Enzyme and hormonal markers in the differential diagnosis of human azoospermia. 153 Mar 67

Impact of thyroidectomy (hypothyroidism) on few glycosidases was studied in the seminal vesicles of young albino rats. Thyroidectomy was performed at 30 days post partum. Seminal vesicular beta-D-glucosidase, beta-D-galactosidase, and N-acetyl-beta-D-galactosaminidase exhibited a similar response of decreased activities under short- (30 days) and long-term (60 days) hypothyroid conditions. On the other hand, N-acetyl-beta-D-glucosaminidase registered a temporal biphasic response of increased and decreased activities in the seminal vesicles of rats subjected to short- and long-term hypothyroidism, respectively. The data obtained in the present study suggest that thyroid hormones have specific influences on different glycosidases in the seminal vesicles of rats and euthyroid status is essential for the maintenance of normal activities of these enzymes.
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PMID:Influence of thyroidectomy on seminal vesicular glycosidases of young albino rats. 187 34

An enzymatic characterization of 16 strains of Aeromonas species including A. hydrophila (7), A. sobria (5), and A. caviae (4) was carried out using API Peptidase (strips numbered 1, 2, 3, 4, 5, and 6); API Esterase and API "Osidase" test strips. A total of 89 substrates was used in the assay and included 59 arylamides (aminopeptides), 10 esters, and 20 carbohydrates. All three species were remarkably uniform in their reactivities. Nineteen (32%) of the arylamide substrates used were hydrolyzed by all three species. Very strong arylamidase activity was displayed by all three species for L-lysine, L-hydroxyproline, L-arginine, L-alanine, L-proline, and L-leucyl-L-alanine. Esterase activity was strongest against caproate (C6), caprylate (C8), nonanoate (C9), and caprate (C10) substrates. Only a limited number of carbohydrate substrates were hydrolyzed; strong N-acetyl-beta-D-glucosaminidase activity was given by all strains. Both A. hydrophila and A. caviae gave strong beta-D-glucosidase reactivities, while A. sobria appeared to be negative for this enzyme. The results of our preliminary study show that some of the enzymes examined may be useful in the identification and differentiation of these species. The API enzyme assays yielded rapid (4 hr) results. The assays were easy to perform, relatively inexpensive and reproducible. The importance of replicate testing and the inclusion of uninoculated (buffer only) controls as part of the assay is emphasized.
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PMID:Enzymatic characterization of three aeromonas species using API Peptidase, API "Osidase," and API Esterase test kits. 307 50

The nephrotoxicity of three different dose levels of propyleneimine (10, 20 and 30 microliter/kg body wt) administered intraperitoneally to rats was studied and 20 microliters/kg body weight was found to be the most appropriate sublethal dose. Injection of propyleneimine (10 microliters/kg body wt) produced a small rise in N-acetyl-beta-D-glucosaminidase (NAG) activity, minor histological damage but no change in urine volume. Six rats were injected with 20 microliters/kg body weight, and urine was collected over the following 16 days. An immediate increase in urine volume, osmolality together with a concomitant decrease in specific gravity, was accompanied by a small increase in creatinine excretion and a more marked increase in the sodium and potassium content of urine after the administration of the nephrotoxin. NAG activity increased immediately and peaked on day 3, the activity remained elevated until day 12 when it fell to near normal levels. The activity of both beta-D-galactosidase and beta-D-glucosidase increased 9 days after administration of the nephrotoxin. In contrast, no consistent change was found in the excretion of the brush border marker enzymes, leucine aminopeptidase (LAP), alanine aminopeptidase (AAP) or alkaline phosphatase (ALP). Proteinuria increased sharply the day after injection and remained abnormal. Increased urinary albumin excretion and the predominance of low molecular weight proteins was demonstrated by sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis. Evidence is presented that propyleneimine exerts its early toxic effect on the renal papilla.
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PMID:Renal toxicity of propyleneimine: assessment by non-invasive techniques in the rat. 309 1

In Creutzfeldt-Jakob disease (CJD), there are prominent ultrastructural alterations of the plasma membrane, which contains many glycolipids and glycoproteins. Glycosidases can degrade glycolipids and glycoproteins. Gangliosides, a subset of glycolipids, are decreased in amount at the terminal stages of CJD, and CJD infectivity is closely associated with membrane rich fractions. We therefore studied 10 glycosidases, and found a statistically significant increase in beta-xylosidase, beta-glucuronidase, N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase activities in CJD. In contrast, alpha-glucosidase, beta-glucosidase, alpha-galactosidase, alpha-mannosidase, alpha-fucosidase, and beta-galactosidase were not significantly changed. The above results are consistent with degenerative membrane changes observed morphologically, and with increased degradation of sugar residues on lipids and/or proteins. These changes may be effected by the accumulation of the CJD agent in cell membranes. We suggest that the higher activities of these enzymes in CJD may be partially responsible for some of the structural and biochemical alterations in CJD infected brains.
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PMID:Cerebral glycosidases in experimental Creutzfeldt-Jakob disease. 328 70


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