从海萝中纯化溴过氧化物酶。

Purification of bromoperoxidase from Corallina pilulifera.

作者信息

Itoh N, Izumi Y, Yamada H

出版信息

Biochem Biophys Res Commun. 1985 Aug 30;131(1):428-35. doi: 10.1016/0006-291x(85)91820-0.

Abstract

Bromoperoxidase was purified from the crude extract of Corallina pilulifera (Corallinaeae, Rhodophyta) and found to be homogeneous upon disc gel electrophoresis by precipitation of ammonium sulfate and sequential column chromatographies of DEAE-Sepharose CL-6B, Sepharose 6B and Cellulofine GC-700m. The purified enzyme did not exhibit optical absorption spectra of a hemoprotein. Therefore, bromoperoxidase of C. pilulifera was completely distinguishable from other haloperoxidases which have heme-irons at the catalytic sites.

摘要

从石花菜（珊瑚藻科，红藻门）的粗提物中纯化得到溴过氧化物酶，通过硫酸铵沉淀以及DEAE-琼脂糖CL-6B、琼脂糖6B和纤维素细粉GC-700m的连续柱色谱法，发现其在圆盘凝胶电泳上呈现均一性。纯化后的酶未表现出血红蛋白的光吸收光谱。因此，石花菜的溴过氧化物酶与其他在催化位点含有血红素铁的卤过氧化物酶完全不同。