J. Hutton, A. Kaplan, S. Udenfriend
Aug 1, 1967
Citations
0
Influential Citations
48
Citations
Journal
Archives of biochemistry and biophysics
Abstract
Abstract The amino acid sequence Gly-Pro-Hyp is unique to and recurs in collagen. In contrast, the sequence Gly-Pro-Pro recurs in the experimentally produced collagenase degradable protein which serves as substrate for the enzyme, collagen proline hydroxylase. The primary structure of substrate reappears to be identical with the primary structure of collagen except for the replacement of hydroxyprolyl by prolyl residues. The quantity of the two tripeptides has been determined in collagenase digests of hydroxylase substrate before and after incubation in an enzyme-dependent, proline hydroxylating system. During incubation, Gly-Pro-Pro sequences of substrate are stoichiometrically converted to the Gly-Pro-Hyp sequences characteristic of natural collagen. Approximately 37% of the total hydroxyproline synthesized in vitro is located in Gly-Pro-Hyp sequences. The hydroxyproline formed is 4-hydroxyproline.