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PMID: 3840018 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

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

The Biochemical journal ·Vol. 229 ·No. 1 ·1985-07-01 ·Pages 189-96

Deák F, Argraves WS, Kiss I, Sparks KJ, Goetinck PF

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 alpha 1(II) and alpha 1(I) procollagens diverged later than alpha 1(I) and alpha 2(I) procollagens.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Cartilage/analysis Chickens Cloning, Molecular DNA Nucleic Acid Hybridization Peptides Procollagen
Chemicals
Peptides Procollagen DNA
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Deák F
Argraves W S
Kiss I
Sparks K J
Goetinck P F
References (26)
26 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2290189
Published
1985-07-01
Pages
189-96
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1145166
Subset
IM
Grants
NICHD NIH HHS · HD09174 · United States
Databases
GENBANK
X02663
External Links
PubMed source DOI: 10.1042/bj2290189 PMC Full Text View journal details
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