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- W1979387670 abstract "Endo-β-N-acetylglucosaminidase H from Streptomyces plicatus can be useful in determining both the molecular weight of the protein moiety of glycoproteins and their inherent number of oligosaccharide chains. In the case of carboxypeptidase Y the molecular mass of the carbohydrate free protein was confirmed as 51,000 daltons. The native enzyme was shown to contain 4 oligosaccharide chains each averaging about 14 mannose residues. On treatment of mung bean nuclease I with the endoglycosidase, the molecular mass decreased from 39,000 to 31,000 daltons. The peptides produced on reduction of this enzyme with thiol were 18,700 and 12,500 daltons, indicating that carbohydrate had been present on both. Penicillium nuclease P1 was decreased in size from 40,000 to 30,000 daltons by the endoglycosidase. Although most of the carbohydrate was removed from each of the native enzymes by the endoglycosidase, denaturation of the glycoproteins was necessary to effect complete removal. Enzyme activitywas not affected by carbohydrate depletion of these glycoproteins, a result consistent with similar studies on other oligosaccharide-containing enzymes." @default.
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- W1979387670 date "1977-10-01" @default.
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- W1979387670 title "The use of endo-β-N-acetylglucosaminidase H in characterizing the structure and function of glycoproteins" @default.
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- W1979387670 doi "https://doi.org/10.1016/0006-291x(77)90512-5" @default.
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