Abstract
The proteins examined do not appear to undergo hydrolytic type of degradation to an appreciable extent in anhydrous solutions of HF, CF 3COOH, SO 2KI, SO 2NH 4CNS and NH 3NH 4CNS. The poorer solvents, SO 2 and NH 3 plus salt, cause the protein to aggregate partially into very stable, water-insoluble semi-crystalline fibers. The remaining water soluble portions are typical gelatins of relatively high molecular weight ( M w = 1 · 10 5). Anhydrous hydrogen fluoride swells collagen and disorients it but probably does not break peptide bonds. The low molecular weight gelatins observed in water solutions of hydrogen fluoride treated collagen probably result from incomplete removal of the hydrogen fluoride before the addition of water to the system. Anhydrous trifluoroacetic acid has essentially the same effect as anhydrous hydrogen fluoride.
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