Ohkudo N, Watabe S, Oshiro T, Takashima F, Nakajima H
Laboratory of Sea-Farming, Tokyo University of Fisheries, Japan.
J Comp Physiol B. 1993;163(6):445-51. doi: 10.1007/BF00346928.
Three hemoglobin components in carp designated CI, CII, and CIII, were isolated by DEAE-Tokyo-pearl ion-exchange chromatography. Constituent globin chains, alpha 1, alpha 2, beta 1, and beta 2, were analyzed by urea-Triton acid polyacrylamide gel electrophoresis and isolated by high performance liquid chromatography with a reverse-phase column. Tryptic peptide mapping indicated that the alpha-globin chains of the three hemoglobin components have slightly different structures. In addition, N-terminal amino acid sequence analysis indicated that the beta 1-globin chain has a primary structure different from that of the beta 2-chain. A series of hybridization experiments between isolated hemoglobins, together with such structural properties of globin chains, suggested that the three hemoglobins have the following compositions: CI (alpha 1 alpha 2 beta 1(2)), CII (alpha 1 alpha 2 beta 1 beta 2), and CIII (alpha 1 alpha 2 beta 2(2)). Hemoglobin CII was a hybrid between the two types each of alpha- and beta-chain and could be constructed in vitro from two hemoglobin components CI and CIII.
通过DEAE - 东京珍珠离子交换色谱法分离出鲤鱼体内的三种血红蛋白成分，分别命名为CI、CII和CIII。通过尿素 - Triton酸聚丙烯酰胺凝胶电泳分析其组成珠蛋白链α1、α2、β1和β2，并使用反相柱通过高效液相色谱法进行分离。胰蛋白酶肽图谱分析表明，三种血红蛋白成分的α - 珠蛋白链结构略有不同。此外，N端氨基酸序列分析表明，β1 - 珠蛋白链的一级结构与β2 - 链不同。分离出的血红蛋白之间的一系列杂交实验，以及珠蛋白链的这种结构特性，表明这三种血红蛋白具有以下组成：CI（α1α2β1(2)）、CII（α1α2β1β2）和CIII（α1α2β2(2)）。血红蛋白CII是α链和β链两种类型各自之间的杂种，并且可以在体外由两种血红蛋白成分CI和CIII构建而成。
