Structure and mode of action of glycoproteins from an antarctic fish

W. Thomas Shier, Yuan Lin, Arthur L. De Vries

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Abstract

The determination of the structures of a series of serum glycoproteins from the Antarctic fish Trematomus borchgrevinki has been completed. These glycoproteins are present in a range of molecular weights and they consist entirely of repeating units of -Ala-Thr-Ala- in which threonine bears a disaccharide moiety that we now show to be a β-d-galactopyranosyl-(1→4)-2-acetamido-2-deoxy-α-d-galactopyranosyl moiety. To our knowledge this represents the first determination of the complete structure of a glycoprotein. These glycoproteins have been shown to be partly responsible for the unusually low temperatures at which the blood serums of Antarctic fishes freeze. We have prepared a series of derivatives of the glycoproteins in which hydroxyl groups of the carbohydrate moiety have been chemically modified by acetonation, acetylation or oxidation. The freezing point depressing activity of the derivatives has been evaluated and the results suggest that the activity results from an interaction with water or ice that involves many structural features of the glycoprotein molecules.

Original languageEnglish (US)
Pages (from-to)406-413
Number of pages8
JournalBBA - Protein Structure
Volume263
Issue number2
DOIs
StatePublished - Apr 15 1972

Bibliographical note

Funding Information:
This work was supported in part by National Science Foundation Grant GV27327, Dernham Junior Fellowship J-I58 from the American Cancer Society, California Division (to W.T.S.), and National Institutes of Health Postdoctoral Fellowship I FO2HE5o4o5-oI (to Y.L.). We thank Dr John Wright of the University of California and Mr R. Kaiser of the Salk Institute for obtaining the NMR spectra, and Dr Y. T. Li of Tulane University for kindly supplying a-and fi-galactosidases.

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