Klimova G I, Gromova L N, Gorkin V Z
Prikl Biokhim Mikrobiol. 1976 Jul-Aug;12(4):614-8.
A substrate of diamine oxidase hexamethylene diamine was covalently bound through adipinic acid dihydrazide to Sepharose 4B in order to prepare a sorbent for the purification of diamine oxidase by means of biospecific (affinity) chromatography. A method was developed to purify diamine oxidase from pig kidney cortex using the sorbent. The method, comprising three steps, yielded enzyme preparations with specific activity 2 000-fold higher than that of kidney homogenate.
为了通过生物特异性(亲和)色谱法制备用于纯化二胺氧化酶的吸附剂,将二胺氧化酶的底物六亚甲基二胺通过己二酸二酰肼共价结合到琼脂糖4B上。开发了一种使用该吸附剂从猪肾皮质中纯化二胺氧化酶的方法。该方法包括三个步骤,得到的酶制剂比肾匀浆的比活性高2000倍。