PMID: 1204602Nov 1, 1975Paper

The covalent structure of collagen. The chymotrypsin, trypsin and hydroxylamine peptides derived from alpha2-CB4 of calf-skin collagen

European Journal of Biochemistry
F W RexrodtK Kühn

Abstract

The cyanogen-bromide-derived peptide alpha2-CB4 from calf skin collagen, consisting of 321 amino acid residues, has been fragmented in order to obtain peptides suitable for automated sequential analysis. Digestion with chymotrypsin liberated six unique peptides consisting of 12, 17, 19, 54, 63 and 156 amino acid residues. Treatment of alpha2-CB4 with hydroxylamine yielded four peptides with 24, 87, 96 and 114 residues. No unspecific cleavage by hydroxylamine was encountered. All of the trypsin-derived peptides of alpha2-CB4 were isolated and characterized by their amino acid compositions. Most of the peptides isolated were ordered along the peptide chain of alpha2-CB4. Ordering of the peptides was greatly assisted by the isolation of double peptides from the chymotrypsin, trypsin and hydroxylamine-derived peptide mixtures.

References

Nov 1, 1975·European Journal of Biochemistry·P P Fietzek, F W Rexrodt
Oct 17, 1972·European Journal of Biochemistry·P P FietzekK Kühn
Sep 1, 1974·European Journal of Biochemistry·P P FietzekK Kühn
Oct 9, 1974·Biochimica Et Biophysica Acta·P P FietzekK Kühn
Aug 21, 1972·Biochemical and Biophysical Research Communications·K A PiezP Bornstein

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Citations

Apr 7, 2010·The Journal of Biological Chemistry·Janice A VrankaHans Peter Bächinger
Nov 1, 1975·European Journal of Biochemistry·P P Fietzek, F W Rexrodt
Aug 5, 2009·Cell Structure and Function·Janice VrankaHans Peter Bächinger
Jan 1, 1995·Critical Reviews in Clinical Laboratory Sciences·D W MossD B Wile

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