Miller J, Wei R
Clin Biochem. 1985 Feb;18(1):14-9. doi: 10.1016/s0009-9120(85)80017-5.
Creatine kinase (EC 2.7.3.2) BB isoenzyme (CK-BB) was purified to homogeneity from canine and human brain tissues. The purified protein from both sources exhibits Mr of 84,700 daltons. The canine isoenzyme exhibits several properties similar to human isoenzyme with respect to reactive and total thiol groups, UV spectra, isoelectric points and reaction kinetics. While both canine and human CK-BB isoenzymes are unstable compared to other CK isoenzymes, canine CK-BB is even less stable than the human enzyme, losing most of its activity within 20 h at 4 degrees C at pH 5.0. Addition of 2-mercaptoethanol does not prevent rapid loss of the enzyme activity. Increasing the pH to 9.0, however, increases the stability of both CK-BB isoenzymes. Agarose electrophoresis demonstrated the presence of MM as well as BB isoenzyme in various parts of brain tissues. BB was present at an activity of 90.8-93.3 U/mg and MM at 6.7-9.2 U/mg.
肌酸激酶(EC 2.7.3.2)BB同工酶(CK-BB)从犬类和人类脑组织中纯化至同质。来自这两种来源的纯化蛋白的分子量为84,700道尔顿。犬类同工酶在反应性和总巯基基团、紫外光谱、等电点和反应动力学方面表现出与人类同工酶相似的几种特性。虽然与其他CK同工酶相比,犬类和人类的CK-BB同工酶都不稳定,但犬类CK-BB比人类酶更不稳定,在pH 5.0的4℃条件下20小时内失去大部分活性。添加2-巯基乙醇并不能阻止酶活性的快速丧失。然而,将pH提高到9.0会增加两种CK-BB同工酶的稳定性。琼脂糖电泳显示在脑组织的各个部位都存在MM以及BB同工酶。BB的活性为90.8 - 93.3 U/mg,MM的活性为6.7 - 9.2 U/mg。