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Cross-linking of Gelatine by Dehydration

Cross-linking of Gelatine by Dehydration THE contribution of water to the stability of macromolecular structures of biological origin is often difficult to assess. Besides its intrinsic theoretical interest1,2, this problem is of great practical importance in studies concerned with the preparation of single crystals of proteins3 and nucleic acids from an aqueous mother liquor as well as in studies of such macromolecules in non-aqueous solvents4. For these reasons we believe that the detailed study of physicochemical changes which accompany the excessive dehydration of proteins and nucleic acids might be of considerable value. In this communication, we wish to report evidence that gelatine becomes covalently cross-linked when the water content falls below about 0.2 g/100 g protein. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

Cross-linking of Gelatine by Dehydration

YANNAS, I. V.; TOBOLSKY, A. V.
Nature , Volume 215 (5100) – Jul 29, 1967
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References (6)

Publisher
Springer Journals
Copyright
Copyright © 1967 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/215509b0
Publisher site
See Article on Publisher Site

Abstract

THE contribution of water to the stability of macromolecular structures of biological origin is often difficult to assess. Besides its intrinsic theoretical interest1,2, this problem is of great practical importance in studies concerned with the preparation of single crystals of proteins3 and nucleic acids from an aqueous mother liquor as well as in studies of such macromolecules in non-aqueous solvents4. For these reasons we believe that the detailed study of physicochemical changes which accompany the excessive dehydration of proteins and nucleic acids might be of considerable value. In this communication, we wish to report evidence that gelatine becomes covalently cross-linked when the water content falls below about 0.2 g/100 g protein.

Journal

Nature – Springer Journals

Published: Jul 29, 1967

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