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The enzymic hydroxylation of protocollagen models
1. Synthetic polymers of l-prolyl-l-prolylglycine of defined chain length, (Pro-Pro-Gly)(n), were found to be substrates for the enzyme protocollagen–proline hydroxylase, with optimum chain length n=5. Boiling the polymer (Pro-Pro-Gly)(15) increased its activity as a substrate but had no effect on (...
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| المؤلفون الرئيسيون: | , , |
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| التنسيق: | مقال |
| اللغة: | English |
| منشور في: |
1969
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| الوصول للمادة أونلاين: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1185139/ https://ncbi.nlm.nih.gov/pubmed/4311063 |
| الوسوم: |
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pubmed-11851392005-09-07 The enzymic hydroxylation of protocollagen models Kikuchi, Y. Fujimoto, D. Tamiya, N. Biochem J Articles 1. Synthetic polymers of l-prolyl-l-prolylglycine of defined chain length, (Pro-Pro-Gly)(n), were found to be substrates for the enzyme protocollagen–proline hydroxylase, with optimum chain length n=5. Boiling the polymer (Pro-Pro-Gly)(15) increased its activity as a substrate but had no effect on (Pro-Pro-Gly)(5). 2. Protection of both or one of the N- and C-terminal groups made (Pro-Pro-Gly)(3) a better substrate, and collagenase digestion of hydroxylated tert.-pentyloxy-carbonyl-(Pro-Pro-Gly)(3) benzyl ester indicated that the central prolyl residues were the major points of hydroxylation. 3. The results suggest that the long-chain peptides are optimum substrates but that a triple-stranded structure is inhibitory for hydroxylation. 1969-11 /pmc/articles/PMC1185139/ /pubmed/4311063 Text en |
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US National Library of Medicine |
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PubMed Central |
| language |
English |
| format |
Article |
| topic |
Articles |
| spellingShingle |
Articles Kikuchi, Y. Fujimoto, D. Tamiya, N. The enzymic hydroxylation of protocollagen models |
| description |
1. Synthetic polymers of l-prolyl-l-prolylglycine of defined chain length, (Pro-Pro-Gly)(n), were found to be substrates for the enzyme protocollagen–proline hydroxylase, with optimum chain length n=5. Boiling the polymer (Pro-Pro-Gly)(15) increased its activity as a substrate but had no effect on (Pro-Pro-Gly)(5). 2. Protection of both or one of the N- and C-terminal groups made (Pro-Pro-Gly)(3) a better substrate, and collagenase digestion of hydroxylated tert.-pentyloxy-carbonyl-(Pro-Pro-Gly)(3) benzyl ester indicated that the central prolyl residues were the major points of hydroxylation. 3. The results suggest that the long-chain peptides are optimum substrates but that a triple-stranded structure is inhibitory for hydroxylation. |
| author |
Kikuchi, Y. Fujimoto, D. Tamiya, N. |
| author_facet |
Kikuchi, Y. Fujimoto, D. Tamiya, N. |
| author_sort |
Kikuchi, Y. |
| title |
The enzymic hydroxylation of protocollagen models |
| title_short |
The enzymic hydroxylation of protocollagen models |
| title_full |
The enzymic hydroxylation of protocollagen models |
| title_fullStr |
The enzymic hydroxylation of protocollagen models |
| title_full_unstemmed |
The enzymic hydroxylation of protocollagen models |
| title_sort |
enzymic hydroxylation of protocollagen models |
| publishDate |
1969 |
| url |
https://ncbi.nlm.nih.gov/pmc/articles/PMC1185139/ https://ncbi.nlm.nih.gov/pubmed/4311063 |
| _version_ |
1760276713073278976 |