The Degradation of Collagen. III. Characterization of Soluble Products of Mild Acid Degradation

Arthur Veis, Delbert N. Eggenberger, Jerome Cohen

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

The soluble protein obtained during the mild thermal and acid dissolution of purified bovine hide collagen which has had no previous pretreatment does not behave as a typical gelatin but is more closely related to native collagen and “procollagen.” The unfractionated soluble collagen is exceedingly polydisperse and consists of molecules ranging in molecular weight from 20 × 106 to less than 1 × 106. The largest fragments are highly asymmetric and have radii of gyration on the order of 6000 Å., deduced from light scattering and viscosity measurements at 40°. The soluble material obtained under a variety of conditions has been fractionated and the molecular parameters of each fraction have been determined. These parameters have been related to the initial phases of the collagen-gelatin transformation process. The stability of collagen solutions at 40° is discussed.

Original languageEnglish (US)
Pages (from-to)2368-2374
Number of pages7
JournalJournal of the American Chemical Society
Volume77
Issue number9
DOIs
StatePublished - May 1 1955

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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