The Effect of Anionic Detergents on Collagens of Mammals and Teleostei.

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Abstract
Collagen of bovine skin (I) when treated with 5% sodium dodecylsulfate (SDS) results in lowered shrinking temp., increased swelling and a minor solubilization. A reversible fixation of SDS on I takes place. The treatment of I with SDS only slightly affects its ionic groups as evident from the fact that the fixation of cationic chromium is not materially altered. Those reagents which for the reaction with I require coordinate bonds give higher values of fixed chromium in the instance of the SDS pretreated I. This is a permanent change. Cod skin collagen II is largely solubilized. The different behavior of I and II indicates that mammalian collagen is stabilized by cross-links on the peptide groups of adjacent chains (H-bonds), supplemented by salt links. Salt links contribute the main organization and stability of collagen of fish. Additional supplementing data was obtained using naphthalenesulfonic acid and polymetaphosphoric acid.