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A new approach for affinity‐based purification of horseradish peroxidase
Biotechnology and Applied Biochemistry ( IF 3.2 ) Pub Date : 2020-02-15 , DOI: 10.1002/bab.1899
Zuleyha Almaz 1 , Aykut Oztekin 2 , Nurgul Abul 3 , Serpil Gerni 3 , Deniz Erel 3 , Seyma Mehtap Kocak 3 , Mehmet Emin Sengül 3 , Hasan Ozdemir 3
Affiliation  

We have developed efficient procedure for isolation of horseradish peroxidase (HRP) using aminobenzohydrazide‐based affinity chromatography. Sepharose 4B‐bounded aminobenzohydrazides are suitable for long‐term use and large‐scale purification. In this study, 26 aminobenzohydrazide derivatives were synthesized, characterized and defined as new HRP inhibitors. In addition, detailed inhibition effects of these molecules on HRP enzyme were investigated. Affinity matrix was formed by bonding aminobenzohydrazides, which exhibited inhibitory activity to sepharose‐4B‐l‐tyrosine. HRP was isolated from crude homogenate in single step and purification factors were recorded as 1,151‐fold (recovery of 8.5%) with 4‐amino 3‐bromo benzohydrazide and as 166.16‐fold (recovery of 16.67 %) with 3‐amino 4‐chloro benzohydrazide.

中文翻译:

一种基于亲和力的辣根过氧化物酶纯化新方法

我们已经开发了使用基于氨基苯甲酰肼的亲和色谱分离辣根过氧化物酶(HRP)的有效程序。Sepharose 4B结合的氨基苯甲酰肼适用于长期使用和大规模纯化。在这项研究中,合成,表征和定义了26种氨基苯甲酰肼衍生物为新型HRP抑制剂。另外,研究了这些分子对HRP酶的详细抑制作用。亲和基质是通过结合氨基苯甲酰肼而形成的,后者对琼脂糖-4B- 1酪氨酸具有抑制活性。从粗匀浆中一步分离HRP,用4-氨基3-溴苯甲酰肼记录纯化因子为1,151倍(回收率8.5%),使用3-氨基4-氯记录为166.16倍(回收率16.67%)。苯甲酰肼。
更新日期:2020-02-15
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