A glycopeptide resistant to exoglycosidases |
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Authors: | Akinori Amemura Ramesh H Shah Om P Bahl Joseph M Merrick |
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Institution: | Department of Biological Sciences, Division of Cell and Molecular Biology, State University of New York at Buffalo, Buffalo, New York 14260 U.S.A.;Department of Microbiology, State University of New York at Buffalo, Buffalo, New York 14214 U.S.A. |
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Abstract: | The carboxyl group of the terminal N-acetylneuraminic acid residue of the glycopeptide, prepared from α1-acid glycoprotein by protease digestion, was esterified with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, and then reduced with sodium borohydride. The reduced glycopeptide, thus prepared, containing the reduced N-acetylneuraminic acid, was resistant to hydrolysis by neuraminidase, and consequently to other exoglycosidases. The penultimate β-d-galactosyl residue of the oligosaccharide chain of the reduced glycopeptide was hydrolyzed by β-d-galactosidase only after the removal of the terminal, reduced, sialic acid by mild hydrolysis with acid. The reduced glycopeptide should be a useful substrate for the assay of endoglycosidases in the presence of exoenzymes. It should also find use as a carbon source in the growth of endoglycosidase-elaborating bacteria. |
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