By C B Anfinsen
ADVANCES IN PROTEIN CHEMISTRY VOL 4.
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Additional info for Advances in Protein Chemistry, 4
In both types of systems the modified protein was present in fibrillar form, as shown by dispersal of floccules in cold dilute alkali and of gels by dilution with water or dilute acid. Dimensions of some fibrils are reported as 140 A. in width and 16,000 A. in length as determined by the electron microscope, showing that many insulin molecules must have associated to form each fibril. It was concluded that the first step in the modification process was formation of fibrils. 85), gelation occurred through loose association of these long chains.
The specific linkages differ from those of gelatin in that they are irreversible and are probably primary chemical bonds. 1. 25%) and constitutes about 4 % of the plasma protein. In some animal plasmas the proportion is somewhat greater. 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).
When a gel set at a given concentration was partially desiccated and then equilibrated in buffer at 5", the swelling (or shrinking, respectively) corresponded to the concentration at which the gel was set, not the concentration after desiccation. Secondary Eeects Attmhtable to Relaxation. When a gel set at ti aon- PROTEIN GELS 33 centration of 23% a t 5" was warmed to 20", then cooled to 5" and swollen to equilibrium, the degree of swelling was the same as for direct swelling without preheating.