The characterization of the γ-component of gelatin

Arthur Veis*, Joan Anesey, Jerome Cohen

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

Fractions rich in the γ- and δ-components of a gelatin extracted from mature bovine corium collagen were obtained by ethanol-water-salt coacervation. These fractions were characterized by light-scattering, viscosity, sedimentation equilibrium, and sedimentation velocity measurements. The molecular weight of the γ-component was established at 350,000 ± 15,000 and that of the δ-component at 1,440,000 ± 50,000. Both gelatins are lateral aggregates of peptide chains. The δ-component is equivalent to a polymer of four γ-gelatin units with a higher intramolecular cross-link density. The γ-gelatin is renaturable and appears to be similar in all respects to γ-troporollagen except in the degree of intramolecular cross-linking which is probably greater in the γ-gelatin.

Original languageEnglish (US)
Pages (from-to)104-110
Number of pages7
JournalArchives of biochemistry and biophysics
Volume98
Issue number1
DOIs
StatePublished - Jul 1962

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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