Rhodes R K, Gibson K D, Miller E J
Biochemistry. 1981 May 26;20(11):3117-21. doi: 10.1021/bi00514a020.
The human alpha 2(V) collagen chain when cleaved with cyanogen bromide yields ten peptides which can be recovered in approximately equimolar quantities. Characterization of the purified peptides with regard to molecular weight and amino acid composition establishes the uniqueness of the peptides and reveals that the alpha 2(V) chain recovered following limited pepsin digestion contain 956 amino acid residues. Possible homologies between the alpha 2(V) peptides and peptides derived from other collagen chains were noted. In addition, a high-performance liquid chromatography system is described for the separation of three of the alpha 2(V) chain peptides which were not resolved by using conventional separation techniques.
人α2(V)胶原链用溴化氰裂解后产生10个肽段，这些肽段可以以近似等摩尔量回收。对纯化肽段的分子量和氨基酸组成进行表征，确定了肽段的独特性，并揭示了有限胃蛋白酶消化后回收的α2(V)链含有956个氨基酸残基。注意到α2(V)肽段与其他胶原链衍生的肽段之间可能存在同源性。此外，还描述了一种高效液相色谱系统，用于分离用传统分离技术无法分离的三个α2(V)链肽段。
