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XL—On the Binding of Acetic Acid by Proteins*

Published online by Cambridge University Press:  11 June 2012

J. K. Candlish  and
G. R. Tristram
J. K. Candlish
Affiliation:
Department of Biochemistry, Faculty of Medicine, University of Malaya, Kuala Lumpur
G. R. Tristram
Affiliation:
Department of Biochemistry, St. Salvator's College, University of St Andrews.
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Extract

Organic acids are working solvents for a number of proteins, notably the collagens. The mechanism of solubilization can be assumed, as a first hypothesis, to consist of a weakening of salt bonds such that chain-chain interactions are lessened and dispersion can occur. However, this cannot be exclusively true since, in the case of the collagen, it has been pointed out (Gustavson 1956) that this protein is soluble in acetic acid (pK=4·76 at 25°C.) and citric acid (pK1 = 3·13; pK2=476; pK3=6·39, at 25°) but not in hydrochloric or mineral acids of equivalent or greater hydrogen ion concentration. The hydrogen ion is thus not the dominant solubilising factor. The same author suggested that the unionized organic acids were bound by peptide bonds of proteins in such a way as to wedge apart the associated chains.

Type
Research Article
Information
Proceedings of the Royal Society of Edinburgh, Section B: Biological Sciences , Volume 70 , Issue 3 , 1969 , pp. 228 - 232
Copyright
Copyright © Royal Society of Edinburgh 1969

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Footnotes

*

This paper was assisted in publication by a grant from the Carnegie Trust for the Universities of Scotland.

References

References To Literature

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