Abstract
The amino acid composition of gelatins from two reptiles, an amphibian and a bird, was determined by ion-exchange chromatography. The agreement in values for gelatin from chicken-leg tendon by both microbiological and ion-exchange methods is very good except for alanine, serine and isoleucine. Chicken-leg tendon gelatin is similar in composition to mammalian materials. The composition of toad-skin gelatin resembles certain fish gelatins more closely than mammalian materials, and the reverse is true for the two reptile gelatins. The realtionship between shrinkage temperature and hydroxyproline and serine plus threonine contents was studied. A very approximate relationship appears to exist between hydroxyproline content and shrinkage temperature.
Keywords