Abstract
1. Collagen was extracted from chick skin with dilute acetic acid followed by dilute acetic acid containing pepsin. 2. The solubilized collagens were purified and portions subjected to further digestion by pepsin. 3. This treatment decreased the aldehyde content but contamination by hexosamine was not diminished. 4. Pepsin treatment converted practically all the acid-soluble collagen into monomeric subunits (α-chains), but the pepsinsolubilized material retained a significant amount of higher subunits (β- and γ-chains). 5. Treatment lowered the rate of fibrillogenesis by acid-soluble collagen, but was without effect on pepsin-solubilized collagen.
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