Primary structure of the telopeptide and a portion of the helical domain of chicken type II procollagen as determined by DNA sequence analysis

F. Deak, W. S. Argraves, I. Kiss, K. J. Sparks, P. F. Goetinck

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

A comparison of the nucleotide sequences of three new cDNA clones for chicken type II procollagen with the sequences of the other three types of chicken fibrillar procollagens reveals that the most conserved regions correlate with the positions of hydroxyproline, hydroxylysine, cysteine and lysine residues. On the basis of replacement-site-divergence calculations it is concluded that α1(II) and α1(I) procollagens diverged later than α1(I) and α2(I) procollagens.

Original languageEnglish
Pages (from-to)189-196
Number of pages8
JournalBiochemical Journal
Volume229
Issue number1
Publication statusPublished - 1985

Fingerprint

Procollagen
Collagen Type II
DNA sequences
DNA Sequence Analysis
Chickens
Hydroxylysine
Hydroxyproline
Lysine
Cysteine
Nucleotides
Complementary DNA
Clone Cells

ASJC Scopus subject areas

  • Biochemistry

Cite this

Primary structure of the telopeptide and a portion of the helical domain of chicken type II procollagen as determined by DNA sequence analysis. / Deak, F.; Argraves, W. S.; Kiss, I.; Sparks, K. J.; Goetinck, P. F.

In: Biochemical Journal, Vol. 229, No. 1, 1985, p. 189-196.

Research output: Contribution to journalArticle

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