Morin L G
Clin Chem. 1976 Jan;22(1):92-7.
I describe a simple, single-tube batch fractionation procedure for separating MM and MB isoenzymes of creatine kinase on a macroporous strong anion exchanger (AG MP-1, Bio-Rad Laboratories). The isoenzymes can be separated in less than 3 min, with a resulting dilution of the serum with no more than an equal volume of buffer. Without sample concentration or spectrofluorometric measurement, the procedure detects 4 U of MB isoenzyme per liter. Sensitivity is limited by the sensitivity and precision of the method of measurement. The CV for the fractionation can be held to less than 4.0% at 65 U of MB per liter. Current fractionation methods are compared to the proposed procedure. With use of a discrete analyzer (Du Pont aca) the mean MB activity in a population free of heart disease was 3.2 +/- 3.0 U/liter (range, 0 to 8 U/liter). The kinetics and stability of isolated isoenzymes are reported, indicating that advisability of storing or pre-incubating samples with mercaptoethanol.
我描述了一种简单的单管批量分馏程序，用于在大孔强阴离子交换剂（AG MP - 1，伯乐公司）上分离肌酸激酶的MM和MB同工酶。同工酶可在不到3分钟内分离出来，血清的稀释体积不超过等体积的缓冲液。无需样品浓缩或荧光光谱测量，该程序可检测到每升4 U的MB同工酶。灵敏度受测量方法的灵敏度和精密度限制。在每升含65 U MB的情况下，分馏的变异系数可保持在4.0%以下。将当前的分馏方法与所提出的程序进行了比较。使用离散分析仪（杜邦aca），在无心脏病的人群中，MB的平均活性为3.2±3.0 U/升（范围为0至8 U/升）。报告了分离出的同工酶的动力学和稳定性，表明用巯基乙醇储存或预孵育样品是可取的。
