Interchain disulfide bonds at the COOH-terminal end of procollagen synthesized by matrix-free cells from chick embryonic tendon and cartilage.
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Matrix-free cells from tendons and cartilage of chick embryos were incubated in suspension, and the procollagens secreted by the cells were isolated in the presence of protease inhibitors. Tendon procollagen was shown to contain both NH 2- and COOH-terminal extensions and interchain disulfide bonds were located in the COOH-terminal region. A disulfide-linked fragment previously isolated after digestion of the molecule with bacterial collagenase was shown to originate from the COOH-terminal end. Cartilage procollagen was also shown to contain interchain disulfide bonds in the COOH-terminal region. © 1976.
author list (cited authors)
Olsen, B. R., Hoffmann, H., & Prockop, D. J
complete list of authors
Olsen, BR||Hoffmann, H||Prockop, DJ