Y. Kikuchi, D. Fujimoto, N. Tamiya
Feb 1, 1969
Citations
0
Influential Citations
7
Citations
Journal
FEBS Letters
Abstract
Hydroxyproline in collagen is synthesized by the hydroxylation of proline residues in protocollagen, a collagen precursor [l] . The hydroxylating enzyme is an oxygenase [2,3] and is purified from chick embryos [4]. The latter authors studied the hydroxylation of polypeptides of various molecular weights, which were synthesized by polymerization of a tripeptide, Lprolylglycyl-Lproline, and fractionated by gel filtration. The molecular weight of the polymerization products had a distribution range. Recently, Sakakibara et al. (including one of the authors) synthesized sequential polypeptides with defined molecular weights by stepwise addition of t-amyloxycarbonyl-L-prolyl-Lprolylglycine on the Merrifield resin [5] . The products, (Lprolyl-L-prolylglycyl), or (Pro-Pro-Gly), , with n values bigger than ten showed a temperature-dependent transition in optical rotation and apparent molecular weight. The phenomenon was not observed with the above nondefined polymers. The transition was ascribed to the conformational change between single chain and triple stranded structures, similar to those observed with collagen [6]. The present paper describes the enzymatic hydroxylation of the products.