Smith D A, Moses G C, Henderson A R
Clin Chem. 1986 May;32(5):758-62.
We examined the stability of human lactate dehydrogenase (EC 1.1.1.27; LD) isoenzymes 1, 2, and 3--purified to specific activities of about 200 kU/g--when lyophilized in a buffered stabilized matrix of bovine albumin. Each isoenzyme was prepared at two activity concentrations and stored at -20, 4, 20, 37, and 56 degrees C for as long as six months. LD-1 activity decayed with zero-order kinetics, LD-2 and LD-3 with first-order kinetics. The extrapolated half-lives of these preparations at -20 degrees C varied between 80 and 530 years. Stability of reconstituted samples stored at 4 degrees C was excellent for LD-1 but poor for LD-2 and LD-3. We suggest that preparations of human LD-1 be further investigated as a possible reference material.
我们检测了人乳酸脱氢酶（EC 1.1.1.27；LD）同工酶1、2和3（纯化至比活性约为200 kU/g）在冻干于牛白蛋白缓冲稳定基质中时的稳定性。每种同工酶均以两种活性浓度制备，并在-20、4、20、37和56℃下储存长达6个月。LD-1活性以零级动力学衰减，LD-2和LD-3以一级动力学衰减。这些制剂在-20℃下的外推半衰期在80至530年之间变化。4℃储存的复溶样品中，LD-1的稳定性极佳，但LD-2和LD-3的稳定性较差。我们建议进一步研究人LD-1制剂作为可能的参考物质。
