The Incomplete Hydroxylation of Individual Prolyl Residues in Collagen
作者： Paul Bornstein
DOI: 10.1016/S0021-9258(18)96002-3
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摘要: Abstract The amino acid compositions of two peptides, obtained from homologous regions the α1 chains rat skin and tail tendon collagen by CNBr cleavage, were found to differ only in their contents hydroxyproline proline. Sequence analyses these each which contained 36 acids, indicated that primary structures prior hydroxylation proline identical prolyl residues susceptible same. However, individual was incomplete both degree several being greater peptide collagen. data indicate structure is heterogeneous as a consequence this hydroxylation, provide preliminary information regarding substrate specificity hydroxylase.
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