Segment-long-spacing aggregates and isolation of COOH-terminal peptides from type I procollagen. Academic Article

abstract

• Type I procollagen secreted by matrix-free cells from chick embryo tendons was purified by DEAE-cellulose chromatography. Electron microscopy of segment-long-spacing aggregates of the procollagen demonstrated the presence of both NH2-terminal and COOH-terminal extensions not found in collagen. The procollagen was digested with bacterial collagenase and the COOH-terminal fragments were isolated by gel filtration and polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Analysis of tryptic peptides demonstrated that the COOH-terminal extensions on the pro alpha 1 and pro alpha 2 chains had different primary structures.

authors

• Prockop, Darwin

published proceedings

• Proc Natl Acad Sci U S A

author list (cited authors)

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

citation count

• 59

complete list of authors

• Hoffmann, HP||Olsen, BR||Chen, HT||Prockop, DJ

publication date

• December 1976

publisher

• Proceedings of the National Academy of Sciences  Publisher

published in

• Proceedings of the National Academy of Sciences of the United States of America  Journal

keywords

• Amino Acid Sequence
• Animals
• Chick Embryo
• Microscopy, Electron
• Peptides
• Procollagen

PubMed Central ID

• 1069985

Digital Object Identifier (DOI)

• 10.1073/pnas.73.12.4304

start page

• 4304

end page

• 4308

volume

• 73

issue

• 12

URL

• http://dx.doi.org/10.1073/pnas.73.12.4304