By C B Anfinsen
ADVANCES IN PROTEIN CHEMISTRY VOL 4.
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Additional resources for Advances in Protein Chemistry, 4
The relaxation of stress observed by Rankine (1904) and Hatschek (1921) is no doubt due to the mobile equilibrium of the cross-links, which dissociate, although slowly, and form again in new places corresponding to unstressed average configurations (cf. Andrews and Tobolsky, 1946). Swelling. The swelling of a network also depends on the concentration of cross-links, as given by Equations 6 and 7, page 15. Qualitatively this treatment of swelling might be expected to be applicable to gelatin gels, even though the interaction between polymer and solvent is much stronger than in the relatively nonpolar systems to which the above equations are intended to apply; and account must be taken of the fact that the cross-links are introduced in the presence of diluent, while subsequent swelling is then observed in equilibrium with excess diluent.
It can be separated from the other proteins by various fractionation procedures, and preparations of as high as 98% purity have been made (Seegers and Smith, 1941; Cohn and others, 1946; Morrison, Edsall, and Miller, 1947). In analyses for purity of such preparations, fibrinogen is defined as the protein recoverable as fibrin after clotting, under conditions in which the conversion to fibrin is known to be complete and the occlusion of other protein by the fibrin is reduced to a minimum (Morrison, 1947).
Explanation of Various Properties. The postulate of a network with cross-links which can be dissociated by raising the temperature, whether they are single or multiple, is useful in interpreting many of the properties of gelatin gels described above. Melting Point. The melting point corresponds to a concentration of cross-links just sufficient to form an incipient network. Qualitatively, for a dimerization equilibrium, this should depend upon concentration in the manner observed. Although Equation 2 could be formally applied to a quantitative calculation, the error introduced in applying it to a diluted system is uncertain, so no attempt will be made to do SO a t the present time.
Advances in Protein Chemistry, 4 by C B Anfinsen