从镰形艾美耳球虫中纯化亮氨酸氨肽酶
Purification of a leucine aminopeptidase from Eimeria falciformis.
作者信息
Kaga M M, Laurent F, Doh A, Luffau G, Yvoré P, Péry P
机构信息
Unité de virologie et immunologie moléculaires, Inra, Jouy-en-Josas, France.
出版信息
Vet Res. 1998 Jan-Feb;29(1):107-11.
PMID:9559525
Abstract
A leucine aminopeptidase was purified from the oocysts of Eimeria falciformis using affinity chromatography and gel filtration techniques. It had a molecular weight of 45-50 kDa. Its maximal activity against leucyl-p-nitro anilide was at pH 8.6. It is a metallo-enzyme highly inhibited by bestatin.
摘要
利用亲和色谱和凝胶过滤技术从镰形艾美耳球虫的卵囊中纯化出一种亮氨酸氨肽酶。其分子量为45 - 50 kDa。它对亮氨酰 - 对硝基苯胺的最大活性在pH 8.6时。它是一种被贝他汀高度抑制的金属酶。
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