Clark C C, Fietzek P P, Bornstein P
Eur J Biochem. 1975 Aug 15;56(2):327-33. doi: 10.1111/j.1432-1033.1975.tb02237.x.
The alpha2 chain of guinea pig skin collagen contains two additional methionyl residues in comparison with the alpha2 chain of other vertebrate species. The order of the three CNBr peptides unique to the alpha2 chain was established on the basis of the homology of their primary structures to sequences of previously ordered regions in the alpha1 and alpha2 chains of other colagens. The two larger peptides, 4A + 4B, were found to correspond to the region homologous to alpha2-CB4 of other species, while the smaller peptide, 3A, was homologous to the NH2-terminal portion of alpha2-CB3. Thus, the order of the peptides in the alpha2 chain of this collagen is 1-O-4A-4B-2-3A-3B-5. Periodate oxidation and alkaline or acid hydrolysis of the CNBr fragments showed that all of the hydroxlysine-linked carbohydrate in the alpha2 chain was present in alpha2-CB4B. Carbohydrate analyses were most consistent with the existence of single monosaccharide and disaccharide units in this region.
与其他脊椎动物物种的α2链相比，豚鼠皮肤胶原蛋白的α2链含有两个额外的甲硫氨酰残基。基于其一级结构与其他胶原蛋白α1和α2链中先前排序区域序列的同源性，确定了α2链特有的三种溴化氰肽的顺序。发现两个较大的肽4A + 4B对应于与其他物种的α2 - CB4同源的区域，而较小的肽3A与α2 - CB3的NH2末端部分同源。因此，这种胶原蛋白α2链中肽的顺序是1 - O - 4A - 4B - 2 - 3A - 3B - 5。溴化氰片段的高碘酸盐氧化和碱或酸水解表明，α2链中所有与羟赖氨酸相连的碳水化合物都存在于α2 - CB4B中。碳水化合物分析与该区域存在单个单糖和二糖单元最为一致。
