THE PREARGININE IN EDESTIN AND ITS RESISTANCE TO HYDROLYSIS

Abstract

The titration data of edestin show that all the arginine found on hydrolysis exists in this protein as "prearginine." The extra ionizable groups of histidine, lysine and tyrosine are free in the quantities found on hydrolysis. Part of the extra carboxyl groups of aspartic and glutamic acids are bound as amides, and 50 per cent are bound in some other manner (perhaps anhydride) leaving only about 6 per cent of these groups free to ionize in edestin. The prearginine in edestin is not converted into arginine on hydrolysis with pepsin up to 18 per cent (of the total hydrolysis). In more highly hydrolyzed solutions it is not possible to detect such a conversion, due to high buffering. Complete hydrolysis however converts prearginine into arginine which can be isolated. Hydrolyzed edestin promotes the growth of sarcomatous fibroblasts about equally well whether 5, 14 or 18 per cent hydrolyzed.