构巢曲霉嘌呤羟化酶I的特性分析
Characterization of purine hydroxylase I from Aspergillus nidulans.
作者信息
Mehra R K, Coughlan M P
机构信息
Agricultural Institute, Moorepark Research Centre, Fermoy, Co. Cork, Ireland.
出版信息
J Gen Microbiol. 1989 Feb;135(Pt 2):273-8. doi: 10.1099/00221287-135-2-273.
PMID:2693595
Abstract
Purine hydroxylase I from Aspergillus nidulans was purified 850-fold. The purified preparations exhibited the spectral and catalytic properties, including broad specificity for oxidizing and reducing substrates, typical of molybdenum/flavin/iron-sulphur-containing hydroxylases (oxotransferases).
摘要
来自构巢曲霉的嘌呤羟化酶I被纯化了850倍。纯化后的制剂表现出光谱和催化特性，包括对氧化和还原底物具有广泛的特异性，这是含钼/黄素/铁硫的羟化酶（氧转移酶）的典型特征。
Zotero 插件