TY - JOUR
T1 - The characterization of the γ-component of gelatin
AU - Veis, Arthur
AU - Anesey, Joan
AU - Cohen, Jerome
N1 - Funding Information:
in part by Grant Institutes of Health,
PY - 1962/7
Y1 - 1962/7
N2 - 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.
AB - 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.
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U2 - 10.1016/0003-9861(62)90152-2
DO - 10.1016/0003-9861(62)90152-2
M3 - Article
AN - SCOPUS:0344401733
SN - 0003-9861
VL - 98
SP - 104
EP - 110
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 1
ER -