Structural and Enzymatical Comparison of Lignostilbene-<i>α,β</i>-dioxygenase Isozymes, I, II, and III, from<i>Pseudomonas paucimobilis</i>TMY1009
作者:Shigehiro Kamoda、Yoshimasa Saburi
DOI:10.1271/bbb.57.931
日期:1993.1
Three isozymes of lignostilbene-alpha,beta-dioxygenase (LSD) from Pseudomonas paucimobilis TMY1009 were separated on QAE-Toyopearl chromatography. All active fractions were further chromatographed on DEAE-Toyopearl, Butyl-Toyopearl, and Sephacryl S-300 columns. Then the isozymes I, II, and III were purified homogeneously. All three isozymes consisted of two subunits with the same mol. mass. According
在QAE-Toyopearl色谱上分离了来自假单胞菌TMY1009的三种木质素-α,β-双加氧酶(LSD)同工酶。所有活性级分均在DEAE-Toyopearl,Butyl-Toyopearl和Sephacryl S-300柱上进行色谱分离。然后将同工酶I,II和III均匀纯化。所有三个同工酶均由具有相同摩尔的两个亚基组成。质量 根据这三个同工酶的N末端氨基酸序列最多25个残基以及肽酶消化的反相HPLC图谱,发现LSD-1,II和III分别由α-α,α-β,和βbeta亚基。他们对二苯乙烯和苯乙烯衍生物的几种底物显示出不同的特异性。