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.
ASJC Scopus subject areas
- Colloid and Surface Chemistry