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- W2026436601 abstract "Abstract [ Lys - 14 C] Protocollagen was isolated from embryonic tendon cells, and examined as a substrate for protocollagen lysyl hydroxylase. The K m for denatured protocollagen was found to be about 10 −18 M, which expressed in terms of molar concentration of the peptide chain. This value is substantially lower than the K m for any of the synthetic peptides tested previously as a substrate for lysyl hydroxylase. The effect of helical conformation of protocollagen on hydroxylysine formation was studied by incubating native and heat-denatured protocollagen with lysyl hydroxylase at 17° C. An inhibiting effect of helical conformation was found in that lysyl residues in native protocollagen were hydroxylated at a markedly lower rate than those in denatured protocollagen. In addition, the relationship between the enzyme concentration and the synthesis of hydroxylysine with native protocollagen deviated from linearity, and the values seemed to be approaching a limit of less than one hydroxylysyl residue per α-chain. The data support th earlier suggestion that formation of a triple-helical structure may be one of the critical factors limiting the hydroxylation of lysyl residues during collagen biosynthesis. To study whether the amino-terminal peptide extensions of protocollagen had any effect on hydroxylation of lysyl residues, the extensions were cleaved off by limited pepsin digestion. The results of hydroxylation experiments were found to be similar whether protocollagen or pepsin-modified protocollagen was used as the substrate." @default.
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- W2026436601 title "Hydroxylation of lysyl residues in native and denatured protocollagen by protocollagen lysyl hydroxylase in vitro" @default.
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- W2026436601 doi "https://doi.org/10.1016/0304-4165(74)90244-x" @default.
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