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Metabolism of hydroxyproline-. cap alpha. -C/sup 14/ in the intact rat. Radioactivity in amino acids from proteins

Journal Article · · J. Biol. Chem.; (United States)
OSTI ID:5696462

DL-Hydroxyproline-..cap alpha..-C/sup 14/ and DL-allohydroxyproline-..cap alpha..-C/sup 14/ were synthesized. After injection into rats, a high level of activity was obtained in the expired carbon dioxide of the animal receiving the allo isomer. One principal liver and one principal urinary metabolite were found, different from each other and different both from ..gamma..-hydroxyornithine and ..gamma..-hydroxyglutamic acid. Urinary hydroxyproline had a specific activity only slightly less than injected hydroxyproline, suggesting the existence of a very small or nonexistent free hydroxyproline pool, though some bound hydroxyproline could be detected in liver protein. The principal labeled amino acid in the liver protein of the animal receiving natural hydroxyproline was alanine, with glutamic and aspartic acids following closely. In the animal which received the allo isomer, glutamic and aspartic acids had the highest activity. Proline, hydroxyproline, glycine, and serine had some, though little, activity. No other radioactive amino acid could be detected. Degradation studies revealed that alanine was derived fairly directly from hydroxyproline. The results suggest that there exists a second pathway to aspartic acid, which then gives rise to glutamic acid.

Research Organization:
Univ. of Illinois, Urbana
OSTI ID:
5696462
Journal Information:
J. Biol. Chem.; (United States), Journal Name: J. Biol. Chem.; (United States) Vol. 223:1; ISSN JBCHA
Country of Publication:
United States
Language:
English