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- W2068879560 abstract "Prolyl-U-14C-sRNA and iminoacyl-U-14C-sRNA (containing hyprolyl-14C- and prolyl-14C-sRNA), prepared from chick-embryos, were separately incubated with microsomal and ribosomal systems. The incubation reactions were carried out under atmospheres of N2 (anaerobic) only or N2 followed by 95% O2:5% CO2, and the incorporation of pro-14C into hot trichloroacetic acid-extractable protein (collagen) was determined. If hyprolyl-sRNA is the precursor of collagen hydroxyproline residues, there should have been a direct transfer of hypro, even under anaerobic conditions, from its sRNA linkages to the templates. When either prolyl-14C- or iminoacyl-14C-sRNA was employed, significant incorporation of hypro-14C was obtained only when anaerobic incubation was followed by aerobic conditions. The incorporation into hypro-14C increased with aerobic incubation time, but it did not require, nor was it enhanced by, the presence of hyprolyl-sRNA in the reaction mixtures. In a second series of experiments, chick-embryo sRNA was fractionated on DEAE-Sephadex columns. As a result, prolyl-14C-sRNA's were prepared which could not be (hydroxylated) converted to hyprolyl-14C-sRNA. The same preparations, when incubated with microsomal systems, did serve as efficient precursors of pro-14C and hypro-14C residues which were incorporated into hot trichloroacetic acid-extractable protein. The evidence obtained indicates that prolyl-sRNA and not hyprolyl-sRNA is the precursor of collagen hydroxyproline residues. The results support the thesis that the hydroxylation of proline occurs after its incorporation into microsomal peptide linkages." @default.
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- W2068879560 date "1966-11-01" @default.
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- W2068879560 title "Hydroxyprolyl-soluble ribonucleic acid and the biosynthesis of collagen" @default.
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- W2068879560 doi "https://doi.org/10.1016/0003-9861(66)90406-1" @default.
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