抄録
Collagen biosynthesis was studied in vivo with special reference to glycine metabolism.
For the purpose, separation of almost all major amino acids in collagen was examined, and a method was established combining group separation of the amino acids by ion exchange chromatography, and separation of the dinitrophenylated amino acids by Celite column chromatography and paper chromato-graphy.
Guinea pigs of different ages were injected with 2-C14-glycine and sacrificed after 3 or 24 hours. Acetic acid extractable skin collagen and serum albumin, which was used as a control protein, were obtained from the animals and purified. After hydrolysis, amino acids of the two proteins were isolated and estimated for their radioactivities. Difference was observed between the two proteins in the pattern of labeling, especially in the ratio of the specific activity of glycine to that of serine, the ratio being 3-5 for collagen and about l for serum albumin, irrespective of the age of the animals and experimental period. The difference of the specific activity ratio may be due to the marked requirement of glycine for collagen biosynthesis, because collagen contains extraordinarily large amount of glycine. Re-lationship between protein biosynthesis and amino acid supplying system was considered.
The authors are grateful to Mr. Y. Mitsui for his co-operation.
