Abstract
The object of this study of the action of sodium periodate and phenyl iodosoacetate on collagen and procollagen was to elucidate the mode of linkage of their carbohydrate components. Both proteins underwent degradation when dissolved in solutions of these 2 reagents (500 mg protein and 250 mg reagent in 50 ml water; periodate at pH 8, iodosoacetate at pH 3.4, both at 40[degree]C for 3 days). The degradation product from collagen behaved as a single substance on electrophoresis (isoelectric point pH 9.2), was not dialyzable, and gelled in dilute solutions. The degradation product from procollagen did not behave as a single substance on electrophoresis, could be dialyzed, and did not gel. In spite of these differences the average chain length (determined chemically or by the Van Slyke method) of the 2 degradation products does not differ significantly. From their behavior with lithium boro-hydride it appears that the terminal carboxyl groups of the procollagen degradation product are free, whereas they are esterified in the corresponding collagen derivative. The amino acid composition of the 2 degradation products using phenyl iodosoacetate was the same as that of the 2 parent proteins.