Burgeson R E, Hebda P A, Morris N P, Hollister D W
J Biol Chem. 1982 Jul 10;257(13):7852-6.
Human hyaline cartilage contains three collagen chains in addition to the alpha 1(II) chain of Type II collagen. Two of these chains, tentatively designated the 1 alpha and 2 alpha chains, have been extensively characterized. Although similar in molecular weight to other collagen chains, by the combined criteria of solubility, electrophoretic mobilities, carboxymethylcellulose elution profiles, total amino acid compositions, carbohydrate contents, cyanogen bromide peptide profiles, limited V8 protease digestion profiles, and examination of selected cyanogen bromide peptides, the 1 alpha and 2 alpha chains are structurally unique collagen alpha chains. Because of similarities of the 1 alpha and 2 alpha chains to the alpha 1(V) and alpha 2(V) chains, respectively., of Type V collagen, specific comparisons between these collagen chains and their constituent peptides were made and yielded the conclusion that these chains are nonidentical, but share substantial similarities.
人透明软骨除了含有II型胶原蛋白的α1(II)链外,还包含三条胶原链。其中两条链,暂定为1α链和2α链,已得到广泛表征。尽管这两条链的分子量与其他胶原链相似,但根据溶解性、电泳迁移率、羧甲基纤维素洗脱图谱、总氨基酸组成、碳水化合物含量、溴化氰肽图谱、有限的V8蛋白酶消化图谱以及对选定溴化氰肽的检测等综合标准,1α链和2α链是结构独特的胶原α链。由于1α链和2α链分别与V型胶原蛋白的α1(V)链和α2(V)链相似,因此对这些胶原链及其组成肽进行了具体比较,得出的结论是这些链并不相同,但有许多相似之处。