Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The specific activities of five glycohydrolases of lysosomal origin (beta-N-acetylglucosaminidase, beta-glucuronidase, beta-galactosidase, alpha-mannosidase and alpha-fucosidase) were measured in different types of primary and metastatic tumors of the human nervous system. The activities of these hydrolytic enzymes in samples of tumor tissue were compared with those in the white matter of 'control' tissue. The specific activities of beta-glucuronidase and beta-N-acetylglucosaminidase were significantly higher (P less than 0.001) in each group of tumors than in normal cerebral matter. The activities of the other hydrolases were sometimes significantly increased in primary tumors, but not always. In metastatic tumors, they were also significantly higher (P less than 0.01).
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PMID:Study of some lysosomal glycohydrolases in tumors of the nervous system. 672 45

The activities of seven different leukocyte hydrolases were studied in 19 patients and ten controls. There was a strong positive correlation between the monocyte count and the activities of the lysosomal enzymes (N-acetyl-beta-glucosaminidase, alpha-fucosidase, beta-galactosidase, and alpha-mannosidase). High alpha-fucosidase and alpha-mannosidase activities were also found in the eosinophilic granulocytes. Using simple commercially available synthetic substrates, it is possible to study the activities of the lysosomal enzymes in different types of leukemias and to recognize the monocytic leukemias even when they present with very immature precursor cells in the peripheral blood.
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PMID:Diagnostic significance of lysosomal enzymes in different types of leukemias. 676 23

Activities of glycosidases neuromanidase, alpha-L-fucosidase, beta-galactosidase and beta-N-acetylglucosaminidase were studied in rat small intestine and liver tissue under conditions of hyper- and hypovitaminosis A. Both excessive and insufficient administrations of vitamin A were accompanied by distinct alterations in activity of the enzymes studied in small intestine and (although less distinct) in liver tissue. The most significant dependence on the presence of vitamin A exhibited beta-galactosidase and especially alpha-L-fucosidase, activity of which was decreased in hypervitaminosis and increased in hypovitaminosis A. Activity of neuraminidase was usually slightly altered but its marked activation was noted in liver tissue under conditions of hypervitaminosis A. Vitamin A appears to participate in allosteric control of the glycosidase activity in small intestine and in catabolism of glycoproteins. The alterations of the enzymatic activity found in hyper- and hypovitaminosis A might be responsible for changes in composition of membrane glycoproteins and, hence, for the typical for vitamin A disbalance impairments in cellular growth and differentiation.
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PMID:[Enzymatic activity of glycoprotein catabolism in the organs of rats with hyper- and hypovitaminosis A]. 677 13

Several glycosidase activities were measured in frontal gray matter of 4 brains from subjects affected by Creutzfeldt-Jakob disease. The changes of N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-glucosidase, alpha-fucosidase and alpha-mannosidase were not statistically significant but significant increases of beta-glucuronidase and beta-galactosidase activities were found. These results are in accordance with several reports on brain glycosidases in scrapie and Semliki Forest virus-infected brain and could explain some changes in brain glycoconjugate content previously observed in human and experimental Creutzfeldt-Jakob disease.
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PMID:Brain glycosidases in Creutzfeldt-Jakob disease. 678 37

Most of the carbohydrate was removed from influenza virus MRC II (H3N2) and its purified hemagglutinin (HA) on treatment with glycosidases, including alpha-mannosidase, beta-N-acetylglucosaminidase, beta-galactosidase and alpha-fucosidase. The release of 50 per cent of the carbohydrate from intact virus particles significantly affected hemagglutinating activity. The ability of untreated and glycosidase-treated virus to inhibit the binding of antibodies directed against the hemagglutinin was almost indistinguishable by competitive radioimmunoassay (RIA). Up to 60 per cent of the carbohydrate from the purified HA of influenza virus could be removed. The antigenicity of glycosidase treated HA molecules decreased 8-fold compared to intact HAs as measured by competitive RIA. In addition, glycosidase digestion of 125I-labeled HA resulted in a decrease in its reactivity in direct RIA. We conclude that the carbohydrate portion of the HA of influenza virus is not of major importance in defining the antigenicity of HA.
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PMID:The role of carbohydrate in determining the immunochemical properties of the hemagglutinin of influenza A virus. 678 4

Automated fluorimetric procedures for the assay of five lysosomal glycohydrolases-beta-N-acetylglucosaminidase; beta-galactosidase; beta-glucuronidase; alpha-mannosidase; alpha-fucosidase-in human plasma were set up. A Carlo Erba autoanalyser CLA 1500, provided with a sampler refrigerating unit and connected with a recording Turner Mod 111 fluorimeter was employed. The automated procedures, under the established optimal conditions, proved to be highly accurate and reproducible. Using the automated assay procedures the effect of sex and age on the plasma levels of the same enzymes was studied. 1273 randomly selected health subjects were studied. No sex differences were observed for all the enzymes studied with the exception of beta-glucuronidase which displayed higher values (about 30%) in males from 25 to 60 years. The developmental profiles of all enzymes in females and males were similar and characterised by: (a) absolute maximum level in the umbilical cord blood; (b) absolute minimum level at 10-14 years; (c) decrease to a second minimum occurring around 35 years (not displayed by beta-galactosidase and by beta-glucuronidase in males); (e) slow further increase up to the elderly level which was then maintained till the oldest age examined, 74 years.
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PMID:Influence of age and sex on five human plasma lysosomal enzymes assayed by automated procedures. 678 8

Simultaneous or sequential treatment of rat adipocytes with neuraminidase plus beta-galactosidase decreased insulin binding by 43%. No modification was observed with either enzyme individually. alpha-Mannosidase enhanced insulin binding (38%), whereas beta-N-acetylglucosaminidase and alpha-L-fucosidase were ineffective. Lectins that interact with galactose (Ricinus communis I, RCAI), mannose, Lens culinaris agglutinin (LCA), Concanavalin A (Con A) or N-acetylglucosamine (wheat-germ agglutinin, WGA) decreased insulin binding by 43, 57, 59 and 85% respectively. Lectin inhibition was dose-dependent, saturable and prevented by specific monosaccharides. RCAI, LCA, Con A and WGA decreased the insulin dissociation process by 45, 90, 78 and 84% respectively. Lectins specific for sialic acid, terminal galactose, N-acetylgalactosamine or fucose (Limulus polyphemus, peanut, soybean and Ulex I agglutinins) did not modify either insulin binding or dissociation. These results indicate involvement of penultimate D-galactose, internal N-acetyl-D-glucosamine and D-mannose residues in both processes. They suggest that, in rat adipocytes, a glycosidic moiety participates in the insulin-receptor interaction through N-linked oligosaccharides of the 'complex type'.
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PMID:Further characterization of the insulin receptor glycosidic moiety in rat adipocytes. 679 21

Autolysis of a homogenate from the human gastric mucosa results in the release of the reducing substances into the supernatant. The activities of the six glycosidases from the human gastric mucosa, N-acetyl-beta-glucosaminidase, N-acetyl-Beta-galactosaminidase, alpha-fucosidase, beta-galactosidase, alpha-mannosidase and alpha-glucosidase were determined. Certain properties of the enzymes are described. The significance of these enzymes in glycoprotein catabolism in the human gastric mucosa is discussed.
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PMID:The degradation of glycoconjugates in the human gastric mucous membrane. 679 8

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

Nine tumour lines with different developmental capacities were derived from spontaneous as well as from one induced teratocarcinoma: three teratocarcinoma-derived rhabdomyosarcomas TDR 602, TDR 694, and TDR 114; two teratocarcinoma-derived neuroblastomas TDN 2151 and TDN 2283; two teratocarcinoma-derived endodermal tumours TDE 274 and TDE 113; one multipotential teratocarcinoma OTT 2289, and one undifferentiated teratocarcinoma OTT 2158. Quantitative analyses of ten catabolic enzymes, i.e. alkaline and acid phosphatase, alpha- and beta-galactosidase, alpha- and beta-glucosidase, alpha-mannosidase, alpha-fucosidase, beta-glucuronidase, and hexosaminidase were carried out at the 20-cell level, and specific enzyme activity profiles were established for each of the tumour lines studied. These profiles may be used for the biochemical identification of a tumour type at the single cell level in addition to morphological and biological criteria.
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PMID:Enzyme activity profiles in mouse teratocarcinomas. A quantitative ultramicroscale analysis. 687 24


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