Structure and Role of Carbohydrate in Freezing Point-depressing Glycoproteins from an Antarctic Fish

作者: Jackie R. Vandenheede , Ahmed I. Ahmed , Robert E. Feeney

DOI: 10.1016/S0021-9258(20)81783-9

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摘要: Abstract The linkage between the galactose and N-acetylgalactosamine of disaccharide attached to every threonine freezing point-depressing glycoproteins from antarctic fish, Trematomus borchgrevinki, has been previously suggested be β, 1–3 or 1–4, rather than 1–6. This paper reports some colorimetric chemical evidence favoring a linkage. Unsubstituted chromogen is formed breakdown upon β elimination with 0.05 m Na2CO3, indicating was proven type by release terminal when small glycopeptides, obtained hydrolysis elastate, were incubated β-galactosidase (Escherichia coli). Enzymatic oxidation C-6 hydroxyls aldehydes oxidase resulted in fully active glycoprotein. activity lost, however, conversion these newly negatively charged groups, either carboxyl groups halogen formation bisulfite addition products.

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