Meerson F Z, Iavich M P
Vopr Med Khim. 1980 Sep-Oct;26(5):599-605.
Three isoenzymes of creatine phosphokinase (CPK) were detected in rat heart myocardium after electrophoretic separation of the enzyme in agarose gel: MM-isozyme, MB-isozyme and BB-isozyme. The ratios of their activities were 60 : 30 : 5. Total activity of CPK per unit mass of myocardium was increased as well as transformation of its isoenzyme spectrum occurred at the early step of heart adaptation to the increased loading caused by aorta contraction. Within the third day of the heart hyperfunction the BB-isozyme activity was as high as 15% in the heart, the hybrid MB-isozyme activity was increased up to 40% and relative activity of the main muscle MM-isozyme was decreased down to 45%. The relative increase in the activity of BB-isozyme appears to reflect the preferable accumulation of the most functionally effective short-living isoenzymes, which play the key role in adaptation of tissues and systems to long-term loading.
在琼脂糖凝胶中对大鼠心脏心肌中的肌酸磷酸激酶(CPK)进行电泳分离后,检测到了三种同工酶:MM同工酶、MB同工酶和BB同工酶。它们的活性比为60:30:5。在心脏适应主动脉收缩引起的负荷增加的早期阶段,每单位质量心肌中CPK的总活性增加,同时其同工酶谱也发生了变化。在心脏功能亢进的第三天,心脏中BB同工酶的活性高达15%,杂合MB同工酶的活性增加到40%,主要的肌肉MM同工酶的相对活性降低到45%。BB同工酶活性的相对增加似乎反映了功能最有效的短寿命同工酶的优先积累,这些同工酶在组织和系统适应长期负荷中起关键作用。