摘要
经超声破碎、硫酸铵分级沉淀、凝胶过滤、磷酸钙胶层析和离子交换层析等步骤，从Ｃｏｍａｍｏｎａｓｔｅｓｔｏｓｔｅｒｏｎｉ菌株中获得了ＳＤＳ－ＰＡＧＥ单一条带，相对分子质量为６２×１０３的间羟苯甲酸４－羟化酶比活提高２１倍，产率为３０％此酶为ＦＡＤ加单氧酶，催化间羟苯甲酸转变为３。
The m-hydroxybenzoate hydroxylase (MOB4-HOase) with 62 000 relative molecular mass from Chmamonas testosteroni was purified to homogeneity upon SDS-PAGE by using sonic crushing, ammonium sulfate fractionation, molecular sieve chromatography, calcium phosphate gel chromatography and ion exchange chromatography. MOB4-HOase has been purified about 21 fold in specific activity with about 30% yield. This enzyme is a FADmonooxygenase to catalyze m-hydroxybenzoate to protocatechuic acid.
出处
《生物化学与生物物理进展》
SCIE
CAS
CSCD
北大核心
1996年第4期337-342,共6页
Progress In Biochemistry and Biophysics
关键词
间羟苯甲酸4
羟化酶
性质
提纯
meta-hydroxybenzoate4- Hydroxylase
purification
characterization
Comamonas testosteroni
