Kamoda S, Saburi Y
Department of Forest Products, Faculty of Agriculture, University of Tokyo, Japan.
Biosci Biotechnol Biochem. 1993 Jun;57(6):931-4. doi: 10.1271/bbb.57.931.
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 to the N-terminal amino acid sequences up to 25 residues of these three isozymes and the reversed-phase HPLC patterns of peptidase-digested them, it was found that LSD-I, II, and III consisted of alpha alpha, alpha beta, and beta beta subunits, respectively. They showed different specificities for several substrates that are stilbene and styrene derivatives.
从少动假单胞菌TMY1009中分离出的木质芪-α,β-双加氧酶（LSD）的三种同工酶在QAE- Toyopearl色谱上进行了分离。所有活性级分进一步在DEAE- Toyopearl、丁基- Toyopearl和Sephacryl S-300柱上进行色谱分析。然后将同工酶I、II和III进行了均一纯化。所有三种同工酶均由两个具有相同分子量的亚基组成。根据这三种同工酶多达25个残基的N端氨基酸序列以及它们经肽酶消化后的反相高效液相色谱图谱，发现LSD-I、II和III分别由αα、αβ和ββ亚基组成。它们对几种作为芪和苯乙烯衍生物的底物表现出不同的特异性。
