The amino acid sequence of chick skin collagen α1-CB7

The presence of a previously unrecognized triplet

John H. Highberger, Clare Corbett, Andrew Kang, Jerome Gross

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Because alignment of the amino acid sequences of chick skin collagen α2-CB3 (1) with the relevant portion of chick skin collagen α1-CB7 (2) suggested that a Gly-X-Y triplet may have been missed in the latter, the peptide TM-2, produced by tryptic digestion of maleylated α1-CB7, was reinvestigated. Cleavage by trypsin at the unblocked lysine at position 18, and isolation of the resulting COOH-terminal peptide, showed this to be a 15-residue peptide containing a previously unrecognized Gly-Pro-Hyp triplet. Sequencing of the peptide showed this to occupy positions 4 through 6, or 56 through 58 of α1-CB7. The latter thus has 271 instead of 268 residues, and the α1[I] chain 1055 instead of 1052.

Original languageEnglish (US)
Pages (from-to)43-49
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume83
Issue number1
DOIs
StatePublished - Jul 14 1978

Fingerprint

Amino Acid Sequence
Skin
Collagen
Amino Acids
Peptides
glycyl-prolyl-hydroxyproline
Trypsin
Lysine
Digestion

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

The amino acid sequence of chick skin collagen α1-CB7 : The presence of a previously unrecognized triplet. / Highberger, John H.; Corbett, Clare; Kang, Andrew; Gross, Jerome.

In: Biochemical and Biophysical Research Communications, Vol. 83, No. 1, 14.07.1978, p. 43-49.

Research output: Contribution to journalArticle

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