Abstract
We have analyzed the hemoglobins of five individual trout from the Ohrid Lake (Salmo L. typicus) by electrophoretic methods, by reversed-phase high-performance liquid chromatography, and by limited structural analyses. The two major classes of hemoglobin are type I (35% of total) and type IV (65%). Type IV is the major oxygen-transporting hemoglobin; it consists of three types of β chain (in about equal quantities) and three types of α chain (one major and two minor types). Several structural differences have been observed between these three β(IV) chains and between the three α(IV) chains, suggesting a complex genetic system governing the synthesis of these proteins. Moreover, a few amino acid substitutions occur at positions involved in contacts between chains, which suggests that differences in oxygen affinity may exist between these various type IV hemoglobins. Type I hemoglobin is less complex because it contains one type of β chain and two α chains; the latter two differ in numerous positions, suggesting duplications of the α(I)-globin gene. The α and β chains of type I hemoglobin differ considerably from the α and β chains of type IV hemoglobin, indicating the existence of α(I)- and β(I)-globin genes separate from the α(IV)- and β(IV)- globin genes.
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This study was supported in part by the Yugoslav-American Joint Funds, pp 812 (to G.D.E.), and by United States Public Health Service Research Grant HLB-05168 (to T.H.J.H.).
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Cepreganova, B., Wilson, J.B., Webber, B.B. et al. Heterogeneity of the hemoglobin of the Ohrid trout (Salmo L. typicus). Biochem Genet 30, 385–399 (1992). https://doi.org/10.1007/BF00569329
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DOI: https://doi.org/10.1007/BF00569329