Trüeb B, Gröbli B, Spiess M, Odermatt B F, Winterhalter K H
J Biol Chem. 1982 May 10;257(9):5239-45.
Type IV collagen was isolated in high yield from bovine kidney cortex. The protein revealed Mr = 380,000 and contained, in a 2:1 ratio, two different disulfide-linked polypeptide chains, C-1 and D-1 (Mr = 125,000). Carboxymethyl-cellulose chromatography before and after reduction proved that the two polypeptide chains are arranged in a single triple helical molecule with the chain composition (C-1)2(D-1). The disulfide bridges appear to be located 180 amino acid residues from the NH2 terminus of the chains.
从牛肾皮质中高产率地分离出IV型胶原蛋白。该蛋白质的相对分子质量为380,000,包含两种不同的以二硫键连接的多肽链C-1和D-1(相对分子质量为125,000),二者比例为2:1。还原前后的羧甲基纤维素色谱分析证明,这两条多肽链以(C-1)2(D-1)的链组成排列在单个三螺旋分子中。二硫键似乎位于距链的NH2末端180个氨基酸残基处。