1966•Journal of Biological ChemistryOpen access

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

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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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What this paper is about

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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Available 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.

Key concepts: Collagenase, Hydroxyproline, Biosynthesis, In vitro, Biochemistry, Chemistry, Protein biosynthesis, Enzyme

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