Studies on Collagen Biosynthesis:Hydroxylation of Proline

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Some of the nature of the substrate for proline hydroxylation was investigated. To prepare the substrate for proline hydroxylation, granuloma minces, obtained from a guinea pig, were incubated with 14C-proline in the presence of α, α'-dipyridyl. After incubation, the minces were washed and then proline-rich polypeptide precursors were extracted with 0.5 N acetic acid. The precursors thus obtained were fractionated by gel filtration through a Sephadex G-200 colum. Analysis of the effluent fractions showed that the first major protein peak contained most of the incorporated proline and is the best substrate for proline hydroxylation among the peaks tested. It was also found that this major peak has a molecular weight of about 100,000 and this value is comparable with that of the α-chain of collagen. Treatment of this fraction with hydroxylamine destroyed about half of the hydroxylating activity. To determine more precisely the nature of the substrate for proline hydroxylation, collagen model peptides, which consist of repeating units of a tripeptide, prolyl-prolyl-glycine (Pro-Pro-Gly), were prepared and the hydroxylation activity was tested with these peptides. The model peptides were synthesized by stepwise polymerization of Pro-Pro-Gly on a chlorobenzyl polystyrene resine as a supporting material. Various sizes of the synthetic (Pro-Pro-Gly) n were incubated with granuloma extract, and it was found that a significant formation of hydroxyproline was observed with (Pro-Pro-Gly) 3,(Pro-Pro-Gly) 5 and (Pro-Pro-Gly) 10, but not with (Pro-Pro-Gly) i. It was also found that the hydroxylation activity is increased in parallel with the increase in the molecular size of the peptides.
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Studies on Collagen Biosynthesis:Hydroxylation of Proline

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