doi: 10.1073/pnas.73.12.4304.
Segment-long-spacing aggregates and isolation of COOH-terminal peptides from type I procollagen
- PMID: 1069985
- PMCID: PMC431440
- DOI: 10.1073/pnas.73.12.4304
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Segment-long-spacing aggregates and isolation of COOH-terminal peptides from type I procollagen
Proc Natl Acad Sci U S A.
1976 Dec.
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.
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