Ayad S, Weiss J B
Biochem J. 1984 Mar 15;218(3):835-40. doi: 10.1042/bj2180835.
The collagens of bovine vitreous-humour and nasal-septum cartilage have been extracted, fractionated and compared. Both tissues show the same heterogeneity of collagen types, consisting of type II, 1 alpha, 2 alpha, 3 alpha and C-PS collagens. The type II collagen of the vitreous humour was significantly more hydroxylated both in the lysine and proline residues than was that of cartilage. C-PS1 collagen, together with higher-Mr forms were present in the vitreous humour, but the higher-Mr forms were not seen in cartilage. Both C-PS1 and C-PS2 were present in vitreous humour and cartilage, but vitreous humour contained three times more of these collagens than did cartilage. Despite the difference in amount, the molar ratio C-PS1/C-PS2 was approx. 1 in both tissues, suggesting that they are components of a larger molecule. The 1 alpha, 2 alpha, 3 alpha collagens were present in the same concentration in both tissues. These three chains co-precipitated on dialysis against phosphate-buffered saline, pH 7.2, in a manner analogous to type V collagen.
已对牛玻璃体和鼻中隔软骨中的胶原蛋白进行了提取、分级分离和比较。两种组织都显示出相同的胶原类型异质性,包括II型、1α、2α、3α和C-PS胶原蛋白。玻璃体中的II型胶原蛋白在赖氨酸和脯氨酸残基上的羟基化程度明显高于软骨中的II型胶原蛋白。C-PS1胶原蛋白以及更高分子量的形式存在于玻璃体中,但在软骨中未见更高分子量的形式。C-PS1和C-PS2都存在于玻璃体和软骨中,但玻璃体中这些胶原蛋白的含量是软骨中的三倍。尽管数量存在差异,但两种组织中C-PS1/C-PS2的摩尔比约为1,这表明它们是一种更大分子的组成部分。1α、2α、3α胶原蛋白在两种组织中的浓度相同。这三条链在pH 7.2的磷酸盐缓冲盐水中透析时共同沉淀,其方式类似于V型胶原蛋白。