Structural changes in collagen. The action of alkalis and acids in the conversion of collagen into eucollagen

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Abstract
Alterations in the structure of collagen by alkali and acid have been assessed by analysis of the N-terminal residues developed. In its least stable form, the collagen fibrillar configuration is unstable in water at 60[degree], transforming into gelatin in a few minutes. This form of collagen is termed "eucollagen" It is suggested that eucollagen relies almost entirely on regions of strong hydrogen-bonding for its molecular stability. The structure of bone collagen is considered to involve chains built from subunits each with number-average chain weight between 60,000 and 70,000. Chain-weight values below 60,000 are not generally encountered for eucollagen. Although HC1 (1.0-2.5 N) does not convert collagen into eucollagen, it can modify the collagen to permit a rapid acceleration of the reaction at pH 12.6. The solution of mucoprotein in acid as well as alkali is noted. The bulk of the mucoprotein present in ossein, which is about 2.2%, is not likely to be a major factor in collagen stability.