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七十年代发展起来的亲和层析技术由于其专一性强,操作简捷,活性回收率高等特点,已经成为分离纯化生物大分子的有效手段。依赖NAD~+的脱氢酶类,特别是乳酸脱氢酶(LDH)同工酶是酶学研究中较为活跃的领域,因此,建立这类酶的亲和层析纯化方法,对于深入研究其结构与功能有着重要的意义。本文参照Lee和Trayerr等人的报导,建立了一种较为简化的8-(6-氨基己基)-5′-AMP-Sepharose 4B亲和吸附剂的合成过程,并利用该吸附剂纯化了家驴,北京鸭,达斡尔黄鼠等不同动物材料中的LDH,取得了好的结果,同时也对几种亲和层析纯化LDH的条件进行了探讨。
The affinity chromatography technology developed in the seventies has become an effective method for separating and purifying biological macromolecules because of its uniqueness, simple operation and high activity recovery rate. Dehydrogenases that rely on NAD ~ +, especially lactate dehydrogenase (LDH) isozymes, are relatively active in the field of enzymology. Therefore, it is necessary to establish affinity chromatography purification methods for these enzymes, Structure and function have important meanings. This paper references Lee and Trayerr et al reported the establishment of a more simplified synthesis of 8- (6-aminohexyl) -5’-AMP-Sepharose 4B affinity adsorbent and the use of the adsorbent purified donkey , Beijing duck, Daurian ground squirrel and other animal materials LDH, and achieved good results, but also to several affinity chromatography purification of LDH conditions were discussed.