Abstract
The isolation and characterization of peptides containing an uncleaved methionyl residue after CNBr cleavage of the α2 chain of chick bone and rat skin collagen show that α2-CB1 and α2-CBO are adjacent and come from the NH 2-terminal end in the order 1-0 and that α2-CB3 and α2-CB5 come from the COOH-terminal end in the order 3–5. These results were confirmed and the remaining two peptides, α2-CB2 and α2-CB4, were positioned by pulse-labeling of rat collagen in culture and isolation of the CNBr peptides in a Dintzis-type experiment. The predicted specific activity gradient along the chain is obtained when the peptides are arranged in the order 1-0-4-2-3-5. These results are in agreement with electron microscopy of the renatured larger peptides α2-CB3, 4 and 5 from chick skin collagen (published in an accompanying article) which shows the order x-4-x-3-5 where x indicates spaces large enough for the remaining smaller peptides.
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