使用亲和洗脱色谱法纯化糖酵解酶。
Purification of glycolytic enzymes by using affinity-elution chromatography.
作者信息
Scopes R K
出版信息
Biochem J. 1977 Feb 1;161(2):253-63. doi: 10.1042/bj1610253.
Abstract
- A systematic procedure for the purification of enzymes by affinity-elution chromatography is described. Enzymes are adsorbed on a cation-exchanger, and eluted with ligands specific for the enzyme concerned. 2. All of the glycolytic and some related enzymes present in rabbit muscle can be purified by the affinity-elution technique. The pH range for adsorption and elution of each enzyme was found, and the effects of minor variations of conditions are described. 3. A description of experimental conditions suitable for affinity elution of each enzyme is given, together with special features relevant to each individual enzyme. 4. Theoretical considerations of affinity elution chromatography are discussed, including its limitations, advantages and disadvantages compared with affinity-adsorption chromatography. Possible developments are suggested to cover enzymes which because of their adsorption characteristics are not at present amenable to affinity-elution procedures.
摘要
- 本文描述了一种通过亲和洗脱色谱法纯化酶的系统程序。酶被吸附在阳离子交换剂上，并用针对相关酶的配体进行洗脱。2. 兔肌肉中存在的所有糖酵解酶和一些相关酶都可以通过亲和洗脱技术进行纯化。确定了每种酶吸附和洗脱的pH范围，并描述了条件微小变化的影响。3. 给出了适合每种酶亲和洗脱的实验条件描述，以及与每种酶相关的特殊特征。4. 讨论了亲和洗脱色谱法的理论考量，包括其局限性、与亲和吸附色谱法相比的优缺点。建议了可能的改进方向，以涵盖由于吸附特性目前不适合亲和洗脱程序的酶。
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