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The α1‐chain of acid soluble calf skin collagen was cleaved with cyanogen bromide, and the resulting peptides were separated by ion exchange and molecular sieve chromatography. Eight different peptides could be isolated as expected from the seven methionyl residues of the chain. Their size was determined by gel filtration, dodecyl sulfate disc electrophoresis, measurement of electron micrographs of renatured peptides, and amino acid analysis. Peptides, differing in length between 19 and 270 residues were found. The C‐terminal peptide α1‐CB6 occurred in two variants (CB6 a and CB6 b ), differing in size, chromatographic behaviour and amino acid composition. The results suggest that CB6 a contains about 15 amino acid residues more than CB6 b . The amino acid compositions of the peptides were in good agreement with the composition of the α1‐chain. All CNBr‐peptides, including the sum of CB6 a and CB6 b , were isolated in approximately equimolar amounts, thus excluding the possibility of repeating sequences within the chain. The order of the CNBr‐peptides was established by electron microscopy and by comparative amino acid analysis of overlapping collagenase derived peptides and uncleaved CNBr‐peptides. It was found to be the same as in α1 from rat skin collagen.
Rauterberg et al. (Thu,) studied this question.