Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The elution profiles of eleven acid hydrolases from human liver and plasma were directly compared using a system whereby a single salt gradient was simultaneously applied to two DEAE-cellulose chromatographic columns. 2. Plasma alpha-L-fucosidase, alpha-mannosidase, alpha-galactosidase and alpha-glucosidase isoenzymes were eluted at higher salt concentrations than the corresponding liver isoenzymes whereasbeta-N-acetylglucosaminidase, beta-galactosidase, beta-glucosidase, exo-1,4-beta-xylosidase and alpha-L-arabinofuranosidase isoenzymes were eluted at lower salt concentrations. The elution profiles of beta-glucuronidase and acid phosphatase weremore complex. 3. After incubation with neuraminidase most plasma hydrolases were eluted at lower salt concentrations, however the elution patterns of beta-glucosidase, beta-xylosidase and acid phosphatase were not altered. 4. Preincubation with neuraminidase had no effect on the elution profiles of six liver hydrolases whereas the major isoenzymes of alpha-mannosidase, beta-galactosidase and alpha-L-arabinofuranosidase were eluted at markedly lower salt concentrations. Liver alpha-fucosidase and alpha-galactosidase were eluted at slightly lower salt concentrations afterincubation with neuraminidase. 5. The results are discussed in relation to thepathogenesis of Mucolipidosis II (I-cell disease), and the synthesis and packaging of lysosomal enzymes.
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PMID:Effect of neuraminidase on the chromatographic behaviour of eleven acid hydrolases from human liver and plasma. 19 Dec 58

Castanospermine (CSP), an inhibitor of alpha-glucosidase, enhanced immunoglobulin (Ig) release in a Staphylococcus aureus Cowan I (SAC)-induced lymphocyte culture (Scand. J. Immunol. 1990. 32: 529). In a pokeweed mitogen (PWM)-human lymphocyte culture, unlike the SAC-stimulated system, CSP strongly decreased the number of IgG-, IgA- and IgM-secreting cells as well as that of Ig-bearing cells. Peripheral blood lymphocytes treated with swainsonine, a mannosidase II inhibitor, or with neuraminidase also showed a reduced response to PWM. In cross-culture experiments, only a mixture of B cells pretreated with either agent and untreated T cells showed such a suppressive effect. Adhesion was decreased between B cells treated with either agent and untreated T cells, but not between treated T cells and untreated B cells. These results demonstrate that a certain alteration in B cell membrane oligosaccharides inhibited the T cell-B cell adhesion in the PWM culture, leading to an arrest of B cell maturation. Considering that these inhibitors eventually prevent terminal sialic acid addition, the present study provides evidence that sialic acids on B cell surface oligosaccharides play a biological role in the T cell-B cell interaction.
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PMID:Glycosidase inhibitors (castanospermine and swainsonine) and neuraminidase inhibit pokeweed mitogen-induced B cell maturation. 163 2

Two fractions of high-molar-mass soluble neutral maltase-glucoamylase (G1 and G2) of distal small intestine of 18-day-old rats separated on Sepharose 4B differ in sialylation which is reflected in their pI values obtained by chromatofocusing. The major soluble G1 fraction shows eight sialylated peaks converted by neuraminidase into a single fraction eluted at pH 4.21. Fraction G2 is less sialylated and neuraminidase causes its pI shift to 4.36. The chromatofocusing pattern suggests that G1 contains more acidic and G2 more basic glycoforms than their membrane-bound counterpart. Presence of less acidic pI values in the soluble G1 fraction of 18-day-old rats than in that of 13-day-old rats indicates that developmental decrease of sialylation concerns not only membrane-bound but also the soluble membrane-type of maltase-glucoamylase.
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PMID:Comparison of sialylation of maltase-glucoamylase in brush-border and soluble fractions of the small intestine of immature rats. 180 96

The activities of 14 lysosomal enzymes in chorionic villi at gestational ages of 6-12 weeks were assayed. Arylsulphatases A and B, alpha-glucosidase and beta-glucuronidase activities increased with advancing gestational age. When compared with the activity in cultured amniotic fluid cells, arylsulphatase A, beta-galactosidase, alpha-glucosidase, heparan N-sulphatase, alpha-L-iduronidase, alpha-mannosidase, neuraminidase, and sphingomyelinase showed significant differences. All except beta-glucuronidase showed lower activity in chorionic villi than in cultured amniotic fluid cells. Prenatal diagnosis using chorionic villi was possible except for alpha-L-iduronidase. Storage at -20 degrees C up to 42 days did not significantly affect activity. The results emphasize the importance of using fresh or frozen age-matched control tissue for diagnosis.
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PMID:Variation of lysosomal enzyme activity with gestational age in chorionic villi. 207 34

The activities of alpha- and beta-glucosidase, beta-galactosidase and beta-N acetylglucosaminidase were assessed at acidic pH by fluorimetry using the appropriate 4-methylumbelliferyl substrate in four Mycoplasma species (M. pneumoniae, M. gallisepticum, M. hominis and M. capricolum) and in Acholeplasma laidlawii. The glycosidase activities were in a low range (0.1-4.2 nmole per h per mg protein) with the exception of higher activities of beta-N-acetylglucosaminidase in A. laidlawii. The enzyme levels of a virulent and a nonvirulent strain of M. pneumoniae were comparable. Despite the very sensitive assay, neuraminidase activity was not detected in M. pneumoniae and M. gallisepticum. No induction of alpha-glucosidase could be demonstrated for M. pneumoniae or A. laidlawii. At least part of the glycosidase activities was localized in the membrane fraction of all mycoplasmas studied. This may support the hypothesis that pathogenic mycoplasmas, being membrane parasites, may modify, by their glycosidases, some host cell glycoconjugates. However, our study did not distinguish the pathogenic mycoplasmas to possess a characteristic glycosidase profile.
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PMID:Glycosidase activities of mycoplasmas. 211 90

The epidermal growth factor receptor in cells of the UMR 106-06 clonal osteoblast line has been shown to be structurally similar to that previously characterized in other cell lines. A specific receptor component of approximately 165,000-185,000 Mr has been identified by polyacrylamide gel electrophoresis using the chemical crosslinker disuccinimidyl suberate to crosslink 125I-EGF to its receptor. Tunicamycin treatment of cells resulted in a dose-dependent loss of binding suggesting involvement of glycosyl moieties in EGF binding to its receptor. Competitive binding studies carried out using wheat germ lectin (WGL), concanavalin A (CON.A.), soybean lectin (SBL), and lentil lectin (ILL) to compete for binding of 125I-EGF revealed that CON A, WGL, and to a lesser extent LL could inhibit EGF binding; SBL was without effect. Treatment of the cells with neuraminidase which cleaves terminal sialic acid residues resulted in total loss of binding while alpha-glucosidase, beta-N-acetylglucosaminidase and alpha-mannosidase were without effect. These data indicate a specific interaction of EGF with terminal sialic acid residues of the EGF receptor. However, it would seem that the mannose residues which appeared to modify EGF binding were not available for the action of the above enzymes due to the presence of sialic acid.
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PMID:Molecular characterization of the EGF receptor and involvement of glycosyl moieties in the binding of EGF to its receptor on a clonal osteosarcoma cell line, UMR 106-06. 300 87

Assay conditions were studied for eleven lysosomal enzymes (beta-D-galactosidase, alpha-D-mannosidase, beta-hexosaminidase, beta-D-glucuronidase, alpha-D-galactosidase, alpha-D-glucosidase, arylsulfatase, beta-D-glucosidase, alpha-L-fucosidase, alpha-D-neuraminidase and alpha-L-iduronidase) in cultured amniotic fluid cells (CAFC), cultured skin fibroblasts (CSF) and cultured embryonic lung fibroblasts (CELF), and the properties of the enzymes were compared among these cultured cells. In addition, changes in these enzymes from the three cell types were investigated between 4-6 earlier passages and 24-26 later passages. With the exception of alpha-D-glucosidase, alpha-D-neuraminidase and alpha-L-fucosidase, all enzymes assayed for the 4-6 earlier passages and the 24-26 later passages had the same Km values and the same pH optima, and were also unchanged with the increasing age of cell cultures, with regard to their points. The specific activities of beta-D-glucuronidase, arylsulfatase, alpha-D-glucosidase and beta-D-glucosidase for the 4-6 earlier passages increased significantly with development, though no change was observed with development in the specific activities of other enzymes. Variations were observed between the levels of these enzymes in the three cell types with the increasing age of cell cultures, such as increases in some, decreases in others and no change in still others.
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PMID:Comparative enzymology of eleven acid hydrolases in cultured amniotic fluid cells, skin fibroblasts and embryonic lung fibroblasts, and the respective changes with the increasing age of the cell cultures. 316 Dec 15

Much of the total genomic variation in eukaryotic organisms may be due to genes other than those coding the primary translation product. Allelic variation, especially as detectable by electrophoresis, in the post-translational processing of enzymes has been briefly reviewed with considerable attention given to a mouse gene (Neu-1) and its pleiotropic effects on several lysosomal hydrolases. Liver acid phosphatase, alpha-mannosidase, arylsulfatase B, and alpha-glucosidase are differentially sialylated as the result of allelic variation for a gene controlling liver neuraminidase activity. Strain SM/J has only 15-20% of the total neuraminidase activity of control strains and is almost totally deficient in the more heat labile of two components of liver activity. The locus controlling this variation (Neu-1) maps very near the D end of H-2 on chromosome 17, apparently within the S region of H-2. A homologous gene has been mapped near the MHC of the rat. The exact nature of the mouse mutant and its relationship to several human diseases characterized by neuraminidase deficiency has not been determined.
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PMID:Post-translational modification of enzymes: processing genes. 635 Feb 18

Giant-cell formation induced by macrophage fusion factor (MFF) was not altered after pretreatment of macrophages with trypsin, chymotrypsin, pronase, neuraminidase, phospholipase C, or phospholipase D. Pretreatment of macrophages with either alpha-mannosidase or alpha-glucosidase completely inhibited giant-cell development, without altering macrophage viability. No alteration of giant-cell formation was observed when 0.1 M of L-fucose, N-acetyl-glucosamine, D-arabinose, D-xylose, melibiose, D-glucose, D-galactose, alpha-lactose, sucrose, D-fructose, or maltose was present during incubation of macrophages with MFF. Giant-cell formation was abolished when 0.1 M alpha-D-mannose was present during macrophage incubation with MFF. These results suggest that the protein moiety of MFF recognizes a specific receptor site on the macrophage membrane, one that is different from those described for other lymphokines and contains alpha-mannose.
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PMID:Chemical nature of the interaction between macrophage fusion factor and macrophage membranes. 635 71

The activities of various glycosidases in homogenates of the small-intestinal mucosa of one adult and two suckling echidnas, Tachyglossus aculeatus, were investigated. The activities of lactase (beta-D-galactosidase), beta-N-acetylglucosaminidase, neuraminidase and alpha-L-fucosidase were higher in the sucklings than in the adult animal. Maltase and isomaltase activities were lower. Sucrase and cellobiase activities were absent or present in trace amounts only. The lactase activity had a pH optimum of 4.0-4.5, was predominantly in the soluble fraction following ultracentrifugation and was inhibited by p-chloromercuribenzene sulfonate, suggesting that it was due to a lysosomal acid beta-galactosidase and not a brush-border neutral lactase. The maltase activity of the sucklings also had the characteristics predominantly of a lysosomal acid hydrolase. It is proposed that in suckling echidnas, the oligosaccharides (mainly neuraminyllactose and fucosyllactose) of the mother's milk are digested intracellularly by lysosomal enzymes, rather than at the brush border, of the epithelial cells of the small-intestinal mucosa.
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PMID:Intestinal glycosidase activities in one adult and two suckling echidnas: absence of a neutral lactase (beta-D-galactosidase). 641 47


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