Flygare S, Griffin T, Larsson P O, Mosbach K
Anal Biochem. 1983 Sep;133(2):409-16. doi: 10.1016/0003-2697(83)90102-1.
Affinity precipitation, a novel technique closely related to immunoprecipitation and affinity chromatography, has been evaluated in systems comprised of dehydrogenases and a bifunctional NAD derivative, Bis-NAD. Lactate dehydrogenase and glutamate dehydrogenase were easily precipitated whereas yeast alcohol dehydrogenase required the presence of salt to enhance the affinity precipitation. Liver alcohol dehydrogenase did not precipitate, probably because most of the affinity complexes formed were composed of only two enzyme molecules. Affinity precipitation was carried out on a preparative scale for the isolation of ox heart lactate dehydrogenase from a crude extract. The yield and purity of the enzyme and the general properties of the procedure are considered very satisfactory.
亲和沉淀是一种与免疫沉淀和亲和色谱密切相关的新技术，已在由脱氢酶和双功能NAD衍生物双-NAD组成的体系中进行了评估。乳酸脱氢酶和谷氨酸脱氢酶很容易沉淀，而酵母乙醇脱氢酶需要有盐存在才能增强亲和沉淀。肝乙醇脱氢酶没有沉淀，可能是因为形成的大多数亲和复合物仅由两个酶分子组成。亲和沉淀以制备规模进行，用于从粗提物中分离牛心乳酸脱氢酶。该酶的产量、纯度以及该方法的一般特性都被认为非常令人满意。
