Human lysosomal alpha-glucosidase. Characterization of the catalytic site
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چکیده
منابع مشابه
Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites.
N-linked glycosylation is one of the important events in the post-translational modification of human lysosomal alpha-glucosidase. Phosphorylation of mannose residues ensures efficient transport of the enzyme to the lysosomes via the mannose 6-phosphate receptor. The primary structure of lysosomal alpha-glucosidase, as deduced from the cDNA sequence, indicates that there are seven potential gly...
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Maltase-glucoamylase (MGAM) and sucrase-isomaltase (SI) belong to human intestinal alpha-glucosidase and their N-terminal side catalytic domains are called NtMGAM and NtSI, and their C-terminal side catalytic domains are called CtMGAM and CtSI. As an antidiabetic, alpha-glucosidase inhibitor is required to bind to all of these domains to inhibit disaccharides hydrolysis. Salacinol and kotalanol...
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heteropoly acids (hpa) and their salts have advantages as catalysts which make them both economically and environmentally attractive, strong br?nsted acidity, exhibiting fast reversible multi-electron redox transformations under rather mild conditions, very high solubility in polar solvents, fairly high thermal stability in the solid states, and efficient oxidizing ability, so that they are imp...
15 صفحه اولHeterogeneity of pig lysosomal acid alpha-glucosidase. Affinity to Sephacryl S-200 gel and tissue distribution.
Acid alpha-glucosidase purified from pig liver showed heterogeneity in its affinity to Sephacryl S-200 gel. Acid alpha-glucosidase was separated into two fractions (S1 and S2) by Sephacryl S-200 affinity chromatography. Each fraction contained components at apparent 76 kDa and 67 kDa on SDS/PAGE. The amount of S1 fraction was about 1.3 times that of the S2 fraction. In the kidney the ratio of S...
متن کاملDisturbance of lysosomal glycogen metabolism by liposomal anti-alpha-glucosidase and some anti-inflammatory drugs.
The size-distribution of liver glycogen was shown to be distinctly affected by the anti-inflammatory drugs salicylate and indomethacin. By measurement of the incorporation of radioactive glucose into glycogen, salicylate was shown to have a depressing effect on overall liver glycogen metabolism. These effects appear to arise from the stabilizing of the lysosome by the drugs. The incorporation, ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)92727-4