文章基本信息

标题：Segment-long-spacing aggregates and isolation of COOH-terminal peptides from type I procollagen
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作者：H P Hoffmann ; B R Olsen ; H T Chen 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1976
卷号：73
期号：12
页码：4304-4308
DOI：10.1073/pnas.73.12.4304
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.