Characterization of the Proα1 Chain of Procollagen ISOLATION OF A SEQUENCE UNIQUE TO THE PRECURSOR CHAIN
作者： Klaus von der Mark , Paul Bornstein
DOI: 10.1016/S0021-9258(19)44107-0
关键词: Cyanogen bromide 、 Sodium dodecyl sulfate 、 Polyacrylamide gel electrophoresis 、 Cysteine 、 Biochemistry 、 Peptide sequence 、 Chemistry 、 Tryptophan 、 Peptide 、 Agarose
摘要: Abstract Radioactively labeled proα1 chains, obtained by culture of embryonic chick cranial bones in the presence [35S]cysteine, were cleaved with cyanogen bromide. A 35S-containing peptide was isolated and purified agarose DEAE-cellulose chromatography. Its molecular weight, determined sodium dodecyl sulfate acrylamide gel electrophoresis, approximately 20,000. Labeling experiments [3H]tryptophan revealed that also contained tryptophan. Comparison amino acid composition weights α1 chains indicated CNBr great majority additional sequence present precursor chain. The this clearly precludes its existence a triple helical conformation.
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