Andrés V, Cussó R, Carreras J
Unitat de Bioquímica, Facultat de Medicina, Universitat de Barcelona, Spain.
Differentiation. 1989 Jul;41(1):72-7. doi: 10.1111/j.1432-0436.1989.tb00734.x.
Phosphoglycerate mutase and creatine phosphokinase have in mammals three isozymes (types MM, MB and BB) with similar tissue distribution and developmental transition in muscle cells. To assess whether the phenotype and the developmental switch of these isozymes differ in the diverse types of muscle fibers, the enzymatic activities and the isozyme patterns, analyzed by cellulose acetate electrophoresis, have been determined in rat soleus, extensor digitorum longus and gastrocnemius muscles during postnatal development. Both phosphoglycerate mutase and creatine phosphokinase activity increased in the three muscles, the increase in extensor digitorum longus and gastrocnemius being higher than in soleus. For the two enzymes the increase in activity was due to the progressive increment of the muscle-specific forms. It is concluded that whereas phosphoglycerate mutase and creatine phosphokinase type-B subunits are present at similar levels in both type I and type II muscle fibers, phosphoglycerate mutase and creatine phosphokinase type-M subunits exhibit much higher levels in type II fibers.
在哺乳动物中，磷酸甘油酸变位酶和肌酸磷酸激酶有三种同工酶（MM型、MB型和BB型），它们在肌肉细胞中的组织分布和发育转变相似。为了评估这些同工酶的表型和发育转换在不同类型的肌纤维中是否存在差异，通过醋酸纤维素电泳分析了大鼠比目鱼肌、趾长伸肌和腓肠肌在出生后发育过程中的酶活性和同工酶模式。在这三种肌肉中，磷酸甘油酸变位酶和肌酸磷酸激酶的活性均增加，其中趾长伸肌和腓肠肌的增加幅度高于比目鱼肌。对于这两种酶来说，活性的增加是由于肌肉特异性形式的逐渐增加。得出的结论是，虽然磷酸甘油酸变位酶和肌酸磷酸激酶的B型亚基在I型和II型肌纤维中的含量相似，但磷酸甘油酸变位酶和肌酸磷酸激酶的M型亚基在II型纤维中的含量要高得多。
