胚胎鸡软骨细胞培养物中二硫键结合的X型前胶原多肽的鉴定。
Identification of disulphide-bonded type X procollagen polypeptides in embryonic chick chondrocyte cultures.
作者信息
Kwan A P, Sear C H, Grant M E
出版信息
FEBS Lett. 1986 Oct 6;206(2):267-72. doi: 10.1016/0014-5793(86)80994-2.
PMID:3758352
Abstract
A high-Mr (Mr 120,000), disulphide-bonded collagenous polypeptide was observed to co-purify with the prox1(X) chain during isolation of cartilage collagens from culture medium of embryonic chick tibiotarsal chondrocytes. This high Mr polypeptide was subsequently shown by two-dimensions l SDS-PAGE and peptide mapping to represent a dimer of the prox1(X) chain of type X collagen linked by disulphide bonding in the non-collagenous domains.
摘要
在从胚胎鸡胫跗关节软骨细胞培养基中分离软骨胶原蛋白的过程中，观察到一种高相对分子质量（相对分子质量为120,000）、二硫键连接的胶原多肽与prox1(X)链共纯化。随后，通过二维SDS-PAGE和肽图谱分析表明，这种高相对分子质量多肽代表了X型胶原蛋白的prox1(X)链在非胶原结构域通过二硫键连接形成的二聚体。
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