A high-resolution acrylamide gel electrophoresis technique for the analysis of collagen polymer components

Charles C. Clark*, Arthur Veis

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

1. 1.|A method of acrylamide-gel electrophoresis using a discontinuous gel system was devised for the analysis of collagen polymer components. 2. 2.|With this method, the α, β, and γ components are well resolved and separate into their distinct regions. A 'pre α' region and a 'higher-polymer' region can also be discerned in some samples. 3. 3.|Comparisons among the gel patterns of three bovine corium collagens (neutral-salt-soluble, acid-soluble, and an alcohol-water-coacervated fraction) have been made by running two samples on the same gel. Differences in the migration rates of similar components of these collagens indicate fundamental differences between the various soluble collagens. 4. 4.|By varying the gel column size and composition, and by making use of the apparent sharpening of boundaries as they pass gel concentration discontinuities, the resolution of this electrophoretic technique can be sufficiently improved so that the differences between both the high and low molecular weight components of similar collagens can be investigated.

Original languageEnglish (US)
Pages (from-to)175-182
Number of pages8
JournalBBA - Protein Structure
Volume154
Issue number1
DOIs
StatePublished - Jan 22 1968

ASJC Scopus subject areas

  • Medicine(all)

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