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From the
1 From the Laboratory of Clinical Biochemistry, National Heart Institute, National Institutes of Health, Bethesda, Maryland, 20014
By use of purified bacterial collagenase it has been possible to demonstrate that a proline-rich, hydroxyproline-deficient, collagenase-degradable protein accumulates in many collagen-forming systems when proline hydroxylation is impaired. These experiments provide further evidence that proline is incorporated into a collagen-like polypeptide prior to hydroxylation. The collagenase-tannic acid procedure may be used as a means of studying collagen synthesis independent of proline hydroxylation.
Submitted on October 14, 1965
This article has been cited by other articles:
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S. Udenfriend Formation of Hydroxyproline in Collagen Science, June 3, 1966; 152(3727): 1335 - 1340. [PDF] |
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