Evidence for a subcellular vesicular site of collagen prolyl hydroxylation

K. R. Cutroneo, N. A. Guzman, Mohamed M.H. Sharawy

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32 Citations (Scopus)

Abstract

The highest specific activity of prolyl hydroxylase in lung tissue was localized in a particulate fraction which was isolated from tissue homogenates by density gradient centrifugation. Electron microscopic studies showed this fraction to be predominantly vesicles with ribosomes studding their surface. Enzymic hydroxylation by this fraction of exogenous substrate prepared from chick embryos required addition of detergent to the enzyme assay mixture. When hydroxylation was inhibited this subcellular fraction also contained proline rich, hydroxyproline deficient substrate which could be hydroxylated in the absence of detergent. These studies indicate a vesicular localization of prolyl hydroxylation and will facilitate future investigations of the intracellular events and regulatory mechanisms involved in collagen synthesis.

Original languageEnglish (US)
Pages (from-to)5989-5994
Number of pages6
JournalJournal of Biological Chemistry
Volume249
Issue number18
StatePublished - Dec 1 1974

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Hydroxylation
Collagen
Detergents
Tissue
Prolyl Hydroxylases
Subcellular Fractions
Density Gradient Centrifugation
Centrifugation
Hydroxyproline
Enzyme Assays
Substrates
Chick Embryo
Ribosomes
Proline
Assays
Electrons
Lung
Enzymes

ASJC Scopus subject areas

  • Biochemistry

Cite this

Evidence for a subcellular vesicular site of collagen prolyl hydroxylation. / Cutroneo, K. R.; Guzman, N. A.; Sharawy, Mohamed M.H.

In: Journal of Biological Chemistry, Vol. 249, No. 18, 01.12.1974, p. 5989-5994.

Research output: Contribution to journalArticle

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