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Identification of a Disulfide-Linked Procollagen as the Biosynthetic Precursor of Chick-Bone Collagen
Janet M. Monson and Paul Bornstein
Proceedings of the National Academy of Sciences of the United States of America
Vol. 70, No. 12, Part I (Dec., 1973), pp. 3521-3525
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/62879
Page Count: 5
You can always find the topics here!Topics: Collagens, Bones, Molecular chains, pH, Elution, Gels, Chromatography, Molecular weight, Molecules, Biosynthesis
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Chick cranial-bone procollagen, extracted at neutral pH in the presence of inhibitors of proteolytic enzymes, exists as a triple-stranded protein with disulfide bonds linking all three chains. The biosynthetic precursor function of this procollagen was demonstrated by pulsechase experiments. The ratio of radioactive hydroxyproline to proline in proα chains obtained by reduction and alkylation of the disulfide-bonded precursor was similar to the value determined for proα 1 from acid-extracted procollagen. However, the molecular weight of these chains was higher than that previously determined for proα 1 and proα 2, suggesting that extraction of tissue at low pH results in a selective loss of disulfide-bonded regions from procollagen. These findings reconcile several apparently conflicting reports on the nature of procollagen identified in bone and in the medium of cultured fibroblasts and indicate that in both systems procollagen is synthesized as a disulfide-linked protein.
Proceedings of the National Academy of Sciences of the United States of America © 1973 National Academy of Sciences