Interchain disulfide bonds at the COOH-terminal end of procollagen synthesized by matrix-free cells from chick embryonic tendon and cartilage. Academic Article

abstract

• 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.

authors

• Prockop, Darwin

published proceedings

• Arch Biochem Biophys

author list (cited authors)

• Olsen, B. R., Hoffmann, H., & Prockop, D. J.

citation count

• 80

complete list of authors

• Olsen, BR||Hoffmann, H||Prockop, DJ

publication date

• January 1976

publisher

• Elsevier  Publisher

published in

• Archives of Biochemistry and Biophysics  Journal

keywords

• Animals
• Cartilage
• Chemical Phenomena
• Chemistry
• Chick Embryo
• Collagen
• Disulfides
• Electrophoresis, Polyacrylamide Gel
• In Vitro Techniques
• Microbial Collagenase
• Microscopy, Electron
• Protease Inhibitors
• Protein Precursors
• Tendons

Digital Object Identifier (DOI)

• 10.1016/0003-9861(76)90516-6

start page

• 341

end page

• 350

volume

• 175

issue

• 1

URL

• http://dx.doi.org/10.1016/0003-9861(76)90516-6