Deyl Z, Rohlicek V, Adam M
Institute of Physiology, Czechoslovak Academy of Science, Prague.
J Chromatogr. 1989 Oct 20;480:371-8. doi: 10.1016/s0021-9673(01)84306-5.
Collagen (types I, II, V, IX and XI) constituting polypeptide chains and their polymers and cyanogen bromide-cleaved peptides of collagen type I and type III were investigated by means of capillary zone electrophoresis. Separations were effected in 2.5 mM sodium tetraborate buffer in less than 15 min. A 50 cm x 0.1 mm I.D. fused-silica capillary was used. The separations were run at 18 kV per capillary. The results of the separation were monitored at 220 nm with an on-tube detection system. Using the Offord equation, relative retention times of cyanogen bromide cleavage fragments were plotted against M(2-3)/Z, where M is the molecular mass of a polypeptide and Z its valency. A linear relationship was observed. Collagen alpha-chains and their polymers were also satisfactorily resolved.
通过毛细管区带电泳研究了构成多肽链的胶原蛋白（I型、II型、V型、IX型和XI型）及其聚合物以及I型和III型胶原蛋白的溴化氰裂解肽。在2.5 mM四硼酸钠缓冲液中进行分离，分离时间不到15分钟。使用内径为0.1 mm、长度为50 cm的熔融石英毛细管。每个毛细管以18 kV的电压进行分离。分离结果通过管内检测系统在220 nm处进行监测。使用奥福德方程，将溴化氰裂解片段的相对保留时间与M(2 - 3)/Z作图，其中M是多肽的分子量，Z是其化合价。观察到线性关系。胶原蛋白α链及其聚合物也得到了令人满意的分离。
