Prabhakaran V, Nealon D A, Henderson A R
Clin Chem. 1979 Jan;25(1):112-6.
In vitro incubation, at 37 degrees C, of human creatine kinase isoenzyme-1 (isoenzyme BB) and human immunoglobulin G in a buffer results in the formation of a complex of high relative molecular mass (Mr approximately 825,000), which contains both proteins. This complex also forms in vitro if creatine kinase isoenzyme-1 is incubated with fresh human serum. The creatine kinase activity of the complex obtained from either incubation is extremely labile, even in the presence of a chelating agent and a thioglycerol. We present evidence for the existence of this complex in the sera of patients who have detectable serum creatine kinase isoenzyme-1 activity. Sera with high activities of creatine kinase isoenzyme-2 do not appear to have this complex. We therefore speculate that complexing of creatine kinase isoenzyme-1 with serum immunoglobulin G may be a pathway of enzyme degradation.
在缓冲液中于37℃对人肌酸激酶同工酶-1（同工酶BB）和人免疫球蛋白G进行体外孵育，会形成一种相对分子质量较高（约825,000）的复合物，该复合物包含两种蛋白质。如果将肌酸激酶同工酶-1与新鲜人血清一起孵育，这种复合物也会在体外形成。从这两种孵育方式获得的复合物的肌酸激酶活性极其不稳定，即使存在螯合剂和硫代甘油也是如此。我们提供证据证明在血清中可检测到肌酸激酶同工酶-1活性的患者血清中存在这种复合物。肌酸激酶同工酶-2活性高的血清似乎没有这种复合物。因此，我们推测肌酸激酶同工酶-1与血清免疫球蛋白G的复合可能是酶降解的一条途径。
