Characterization of the hemoglobins and globins of Synbranchus marmoratus Bloch, 1795 (Pisces, Synbranchidae)

Total hemolysates of Synbranchus marmoratus Bloch, 1795, captured in Vitoriana, district of Botucatu, State of S?o Paulo, Brazil, were submitted to agar-starch gel electrophoresis on glass slides using 42 mM-Tris 1.7 mM EDTA-6.1 mM borate buffer, pH 8.8, for the gel and 10 mM borate-1.7 mM NaOH buffer, pH 8.6, for the cuvette. Three distinct hemoglobin bands were detected, with Hb I being of the cathodic type. Cellulose acetate electrophoresis in 800 mM Tris-2.1 mM EDTA buffer, pH 8.9, containing 6 M urea and 2.25 mM beta-mercaptoethanol indicated the presence of four globin chains denoted alpha 1, alpha 2, beta and gamma. It is suggested that the probable tetrameric constitution of the hemoglobin of Synbranchus marmoratus Bloch, 1795 is Hb I (alpha (2)2 gamma 2), Hb II (alpha (1)2 gamma 2) and Hb III (alpha (1)2 beta 2).