通过钙调蛋白亲和层析法纯化大戟乳胶过氧化物酶。
Purification of Euphorbia characias latex peroxidase by calmodulin-affinity chromatography.
作者信息
Pintus Francesca, Mura Anna
机构信息
Department of Applied Sciences in Biosystems, University of Cagliari, Monserrato, Cagliari, Italy.
出版信息
Ital J Biochem. 2007 Mar;56(1):1-5.
PMID:17511348
Abstract
A new procedure to purify to homogeneity an Euphorbia characias latex peroxidase is performed employing a calmodulin-Sepharose column as affinity chromatography. The advantage of this approach is the isolation of a peroxidase under fast and mild elution conditions with a high recovery in total activity.
摘要
采用钙调蛋白-琼脂糖柱作为亲和色谱，进行了一种将大戟乳胶过氧化物酶纯化至同质的新方法。这种方法的优点是在快速温和的洗脱条件下分离出过氧化物酶，总活性回收率高。
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