Weng M, Pfeifer O, Krauss S, Lingens F, van Pée K H
Institut für Mikrobiologie, Universität Hohenheim, Stuttgart, FRG.
J Gen Microbiol. 1991 Nov;137(11):2539-46. doi: 10.1099/00221287-137-11-2539.
Two non-haem bromoperoxidases (BPO 1 and BPO 2) were purified from the 7-chlorotetracycline-producing strain Streptomyces aureofaciens ATCC 10762. Both enzymes showed azide-insensitive brominating activity, and bromide-dependent peroxidase activity. BPO 1 was a dimer (Mr 65,000) with subunits of identical size (Mr 31,000). The pI was estimated to be 4.5. The enzyme did not cross-react with antibodies raised against the non-haem bromoperoxidase (Mr 90,000) from S. aureofaciens Tü24, a strain that also produces 7-chlorotetracycline. The Mr of BPO 2 was estimated to be 90,000. The enzyme had three identical subunits (Mr 31,000), and its isoelectric point was 3.5, identical with that of the bromoperoxidase from S. aureofaciens Tü24. Moreover, BPO 2 was immunologically identical with the bromoperoxidase from S. aureofaciens Tü24, although both it and BPO 1 could be distinguished electrophoretically from the latter bromoperoxidase.
从生产7-氯四环素的金色链霉菌ATCC 10762中纯化出两种非血红素溴过氧化物酶(BPO 1和BPO 2)。这两种酶均表现出对叠氮化物不敏感的溴化活性以及依赖溴化物的过氧化物酶活性。BPO 1是一种二聚体(Mr 65,000),其亚基大小相同(Mr 31,000)。估计其pI为4.5。该酶与针对同样生产7-氯四环素的金色链霉菌Tü24的非血红素溴过氧化物酶(Mr 90,000)产生的抗体不发生交叉反应。BPO 2的Mr估计为90,000。该酶有三个相同的亚基(Mr 31,000),其等电点为3.5,与金色链霉菌Tü24的溴过氧化物酶相同。此外,BPO 2与金色链霉菌Tü24的溴过氧化物酶在免疫学上相同,尽管它和BPO 1在电泳上都可与后一种溴过氧化物酶区分开来。