Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

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
Stable URL: http://www.jstor.org/stable/62879
Page Count: 5
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Identification of a Disulfide-Linked Procollagen as the Biosynthetic Precursor of Chick-Bone Collagen
Preview not available

Abstract

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.

Page Thumbnails

  • Thumbnail: Page 
3521
    3521
  • Thumbnail: Page 
3522
    3522
  • Thumbnail: Page 
3523
    3523
  • Thumbnail: Page 
3524
    3524
  • Thumbnail: Page 
3525
    3525