van Der Rest M, Cole W G, Glorieux F H
Biochem J. 1977 Mar 1;161(3):527-34. doi: 10.1042/bj1610527.
Samples (1-2mg) of purified human type I, II and III collagens and alpha1(I) and alpha2 chains were digested with clostridiopeptidase A and the released peptides analysed by ion-exchange high-pressure liquid chromatography. Specific 'fingerprints' were produced for each type of collagen. The reproducible nature of these 'fingerprints' and the reconstitution of the type I 'fingerprint' from the 'fingerprints' of the component alpha1(I) and alpha2 chains showed that the specificity of these 'fingerprints' was related to the primary structure of each type of collagen. In addition, some of the differences observed between the 'fingerprints' of the alpha1(I) and alpha2 chains of type I collagen were shown to be suitable for the quantitative analysis of these chains.
将纯化的人I型、II型和III型胶原蛋白以及α1(I)和α2链的样品(1 - 2毫克)用梭菌肽酶A消化,释放的肽通过离子交换高压液相色谱进行分析。每种胶原蛋白都产生了特定的“指纹图谱”。这些“指纹图谱”的可重复性以及由组成α1(I)和α2链的“指纹图谱”重构I型“指纹图谱”表明,这些“指纹图谱”的特异性与每种胶原蛋白的一级结构有关。此外,I型胶原蛋白α1(I)和α2链的“指纹图谱”之间观察到的一些差异被证明适用于这些链的定量分析。