The Effects of Acetic Acid on Collagen Cross-Links

Abstract
Native, acid-soluble and acid-insoluble collagen from the tail tendons of rats and calves have been reduced by 3H-sodium borohydride. The reduced cross-link derivatives were separated by ion exchange chromatography. The destruction of the cross-links under the conditions of hydrolysis was measured. By applying the appropriate correction factors, the approximate levels of the respective cross-link structures in the variously treated tissues were assessed. We conclude that treatment of collagen by 0.05 M acetic acid for 1 hour or less imposes a profound rearrangement of intermolecular bonds in both the soluble and insoluble preparations. The nature of the intermolecular bonding in native collagen therefore cannot be meaningfully assessed if the preparation is previously exposed to acid.

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