High Molecular Weight a Chains in Acid-Soluble Collagen and Their Role in Fibrillogenesis

C. C. Clark*, A. Veisi

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


Denatured acid-soluble collagens from bovine and rat skins contain fractions which do not elute in the salt gradient in the usual carboxyrnethyl (CM)-cellulose chromatographic systems at 40°. These fractions are eluted with 6.0 m urea. Once isolated, these fractions show enhanced aggregation and renaturation properties typical of the crosslinked collagens. They can be dissociated into their constituent peptide chains by dénaturation at 60° and the chains separated by CM-cellulose chromatography at elevated temperature. The chains so prepared have compositions different from the a 1 and al components and, as demonstrated by disc gel electrophoresis and analytical ultracentrifugation have molecular weights 10-30% higher than α1 and α1. The composition data lead to the suggestion that the urea-eluted fractions represent a chains and polymers containing peptide extensions of noncollagen character directly adjoining the peptide chain backbones. The ureä-eluted fractions renature to native fibril form and, in the presence of ATP, form very thin segment long spacing type precipitates showing a marked 300 A head-to-tail overlap in contrast to the usual segment long spacing single spool precipitates seen in unfractionated acid-soluble collagens. It is proposed that the peptide extensions assist in the alignment and organization of monomeric collagen into the limiting microfibrils characteristic of native collagen fibers.

Original languageEnglish (US)
Pages (from-to)494-502
Number of pages9
Issue number4
StatePublished - Feb 1 1972

ASJC Scopus subject areas

  • Biochemistry

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