Segment-long-spacing aggregates and isolation of COOH-terminal peptides from type I procollagen.
- 1 December 1976
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 73 (12) , 4304-4308
- https://doi.org/10.1073/pnas.73.12.4304
Abstract
Type I procollagen secreted by matrix-free cells from chick embryo tendons was purified by DEAE-cellulose chromatography. EM 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.This publication has 25 references indexed in Scilit:
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