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通过亲和柱色谱法从鸡卵黄中纯化腺苷脱氨酶。

Purification of adenosine deaminase from chicken-egg yolk by affinity column chromatography.

作者信息

Lopez R, Cabre F, Franco R, Cascante M, Canela E I

机构信息

Department of Biochemistry and Physiology, Faculty of Chemistry, University of Barcelona, Catalonia, Spain.

出版信息

Prep Biochem. 1990;20(3-4):199-204. doi: 10.1080/00327489008050196.

Abstract

Adenosine deaminase (adenosine aminohydrolase; E.C. 3.5.4.4) has been purified 4686-fold from egg yolk. The procedure developed was used to isolate the enzyme from eight chicken eggs. An easily prepared affinity column employing purine riboside was used as the final step in the purification. The method developed permits the rapid isolation and a high recovery of the protein. The specific activity of the enzyme preparation obtained is 81.4 mU/mg.

摘要

腺苷脱氨酶(腺苷氨基水解酶;E.C. 3.5.4.4)已从蛋黄中纯化了4686倍。所开发的方法用于从八个鸡蛋中分离该酶。采用嘌呤核糖苷的易于制备的亲和柱用作纯化的最后一步。所开发的方法能够快速分离并高回收率地获得该蛋白质。所获得的酶制剂的比活性为81.4 mU/mg。

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