Multiple hemoglobins in Triturus cristatus: their study by analytical isoelectrofocusing.
Electrophoretic separation of the hemoglobin of healthy adult Triturus cristatus reveals four components. Isoelectric focusing of the same hemolysates in various commercial ampholytes of different chemical composition and pH range results in the separation of eight individual hemoglobin bands. The bands obtained by electrophoresis are not homogeneous as revealed by individual gel electrofocusing. They finally separate into the same eight components, as in the whole hemolysate. From the above findings it is concluded that this species has not four but eight individual hemoglobin molecular forms. Our results demonstrate lack of hemoglobin polymorphism in this species.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000302:isolation & purification*; D006461:Hemolysis; D007525:Isoelectric Focusing / Q000379:methods; D014319:Triturus / Q000097:blood*
D006454:Hemoglobins