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. 1976 Dec;73(12):4304–4308. doi: 10.1073/pnas.73.12.4304

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

H P Hoffmann, B R Olsen, H T Chen, D J Prockop
PMCID: PMC431440  PMID: 1069985

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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