Hombrados I, Rodewald K, Allard M, Neuzil E, Braunitzer G
Biol Chem Hoppe Seyler. 1987 Feb;368(2):145-54. doi: 10.1515/bchm3.1987.368.1.145.
Erythrocytes of the adult Sea Lamprey Petromyzon marinus contain several haemoglobin species, but only the main constituent has hitherto been sequenced. The present paper describes the determination of the primary structures of the two minor species, whose electrophoretic mobilities are higher and lower than that of the main component. Tryptic peptides from both chains were purified by high-performance liquid chromatography, then sequenced and aligned by homology with the main haemoglobin. The fast and the major components appeared to be very similar, differing in only four positions (pos. 5: Ser----Thr; pos. 33: Thr----Ser; pos. 86: Val----Ala; pos. 99: Gly----Arg). The slow haemoglobin component, however, differed from the main component with respect to 27 amino-acid residues. The position of the three globins of Petromyzon marinus in the phylogenetic tree of haemoglobins is discussed and a relationship with primitive alpha-chains is postulated.
成年海七鳃鳗（Petromyzon marinus）的红细胞含有几种血红蛋白，但迄今为止仅对其主要成分进行了测序。本文描述了两种次要血红蛋白的一级结构的测定，这两种次要血红蛋白的电泳迁移率高于和低于主要成分。通过高效液相色谱法纯化两条链的胰蛋白酶肽，然后进行测序，并与主要血红蛋白进行同源比对。快速成分和主要成分似乎非常相似，仅在四个位置存在差异（第5位：丝氨酸→苏氨酸；第33位：苏氨酸→丝氨酸；第86位：缬氨酸→丙氨酸；第99位：甘氨酸→精氨酸）。然而，慢速血红蛋白成分与主要成分在27个氨基酸残基上存在差异。讨论了海七鳃鳗的三种球蛋白在血红蛋白系统发育树中的位置，并推测了其与原始α链的关系。
