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J. Biophys. and Biochem. Cytol., Vol 10, 373-388, Copyright © 1961 by Rockefeller University Press

ARTICLE

MORPHOLOGICAL AND CHEMICAL STUDIES OF COLLAGEN FORMATION

: II. Metabolic Activity of Collagen Associated with Subcellular Fractions of Guinea Pig Granulomata



D. A. Lowther Ph.D.1, N. M. Green Ph.D.1, and J. A. Chapman Ph.D.1

1 From the Department of Chemical Pathology, St. Mary's Hospital Medical School, London, England, and the Rheumatism Research Centre, University of Manchester, England.

Dr. Lowther's present address is Department of Microbiology, John Curtin School of Medicine, Australian National University, Canberra, Australia

Electron micrographs of thin sections of nuclear, microsomal, and mitochondrial fractions obtained from a carrageenin-induced granuloma showed considerable contamination of the heavier by the lighter fractions. Striated collagen fibrils could be identified in the nuclei + debris fraction. Only a few striated fibrils occurred in the mitochondrial fraction; very fine filaments (diameter 50 A) could be seen in this fraction, but could not be distinguished with certainty from fibrillar material derived from broken nuclei. 35 per cent of the mitochondrial and 80 per cent of the microsomal collagen was extractable by 0.2 M NaCl and could be purified by the standard methods of solution and reprecipitation. The amino acid composition of these collagen fractions determined by ion exchange chromatography was within the range normally found for collagen and gelatin from other mammalian species, allowing for 10 to 20 per cent of some non-collagenous contaminant of the microsomal collagen. Hydroxyproline and proline were isolated by chromatography on paper from hydrolysates of the nuclear, mitochondrial, and microsomal collagen fractions, after incubation of tissue slices with L-14C-proline. The specific activities of the hydroxyproline from these collagens were in the approximate ratio 1:2:6, while that of bound hydroxyproline derived from the supernatant was only 1, indicating primary synthesis of collagen in the microsomes. Attempts to demonstrate incorporation of L-14C-proline into collagen or into free hydroxyproline in cell free systems were unsuccessful, nor was it possible to demonstrate non-specific incorporation of L-14C-valine into TCA-insoluble material by various combinations of subcellular fractions.

Submitted on September 14, 1960


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