Koussoulakos S, Kaparos G, Stathakos D
Comp Biochem Physiol B. 1986;83(2):475-81. doi: 10.1016/0305-0491(86)90398-6.
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.
对健康成年欧洲火蝾螈血红蛋白进行电泳分离，可得到四种成分。在不同化学成分和pH范围的各种商业两性电解质中，对相同的溶血产物进行等电聚焦，可分离出八条单独的血红蛋白带。如通过个体凝胶电聚焦所示，电泳得到的条带并非均匀一致。它们最终分离成与全溶血产物中相同的八种成分。从上述发现可以得出结论，该物种并非有四种而是有八种单独的血红蛋白分子形式。我们的结果表明该物种不存在血红蛋白多态性。
