Primary structure of hemoglobin from trout (Salmo irideus) amino acid sequence of the beta chain of trout Hb I.

The amino acid sequence of the beta chain of trout Hb I is presented; it adds to the previously reported sequence of the alpha chain (Bossa et al. (1978) Biochim. Biophys. Acta 536, 298-305), thus completing the primary structure of the hemoglobin component of trout's blood devoid of heterotropic phenomena. Comparison of beta chain from trout Hb I with the corresponding sequences from human and carp shows differences of 46.6% and 34.7%, respectively; the sequence (almost completed) of the beta chain from the other major hemoglobin component of trout, i.e., trout Hb IV, displays more differences (41.6%) from beta trout Hb I than from the corresponding chain of other fishes, such as carp or goldfish.