Petruzzelli R, Barra D, Sensi L, Bossa F, Brunori M
Dipartimento di Scienze Biochimiche, Università di Roma La Sapienza, Italy.
Biochim Biophys Acta. 1989 May 1;995(3):255-8. doi: 10.1016/0167-4838(89)90043-5.
The amino acid sequence of the alpha-chain of trout hemoglobin (Hb) IV is given, thus completing the primary structure of the hemoglobin component of trout's blood characterized by the Root effect. The trout Hb IV alpha-chain consists of 142 amino acid residues; comparison with the corresponding sequences from human and carp hemoglobins shows differences of 50.0 and 35.9%, respectively. A difference of 39.6% is found with the alpha-chain of trout Hb I, the other major hemoglobin component of trout blood, devoid of heterotropic effects.
给出了鳟鱼血红蛋白(Hb)IVα链的氨基酸序列,从而完成了以鲁特效应为特征的鳟鱼血液血红蛋白成分的一级结构。鳟鱼Hb IVα链由142个氨基酸残基组成;与人类和鲤鱼血红蛋白的相应序列比较,差异分别为50.0%和35.9%。与鳟鱼血液中另一种主要血红蛋白成分、无异源效应的鳟鱼Hb I的α链相比,差异为39.6%。