Further Evidence for the Accumulation of a Hydroxyproline-deficient, Collagenase-degradable Protein during Collagen Biosynthesis in Vitro
A. Arthur Gottlieb, Arnold P. Kaplan, Sidney Udenfriend
Abstract
A. Arthur Gottlieb, Arnold P. Kaplan, Sidney Udenfriend
Abstract
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.
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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.
Key concepts: Collagenase, Hydroxyproline, Biosynthesis, In vitro, Biochemistry, Chemistry, Protein biosynthesis, Enzyme