Purification of Euphorbia characias latex peroxidase by calmodulin-affinity chromatography.

The Italian journal of biochemistry Pub Date : 2007-03-01
Francesca Pintus, Anna Mura
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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.

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钙调素亲和层析纯化大大麻乳胶过氧化物酶。
采用钙调素- sepharose为亲和层析柱,建立了一种纯化大大麻乳胶过氧化物酶的新方法。该方法的优点是在快速和温和的洗脱条件下分离过氧化物酶,总活性回收率高。
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