van Pée K H, Lingens F
J Gen Microbiol. 1985 Aug;131(8):1911-6. doi: 10.1099/00221287-131-8-1911.
A bromoperoxidase has been isolated and purified from the chloramphenicol-producing actinomycete Streptomyces phaeochromogenes. The purified enzyme was homogeneous as determined by polyacrylamide gel electrophoresis. The prosthetic group of the bromoperoxidase was ferriprotoporphyrin IX. Based on gel filtration results the molecular weight of the enzyme was 147 000 +/- 3000. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis showed a single band having the mobility of a 72 500 molecular weight species. Therefore, in solution at neutral pH, the bromoperoxidase behaved as a dimer. The isoelectric point was 4.0. The spectral properties of the native and reduced enzyme are reported. The homogeneous enzyme also had peroxidase and catalase activity.
已从产氯霉素的放线菌嗜铬链霉菌中分离并纯化出一种溴过氧化物酶。通过聚丙烯酰胺凝胶电泳测定，纯化后的酶呈均一状态。该溴过氧化物酶的辅基为高铁原卟啉IX。根据凝胶过滤结果，该酶的分子量为147 000±3000。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳显示出一条具有72 500分子量物种迁移率的单一谱带。因此，在中性pH的溶液中，溴过氧化物酶表现为二聚体。其等电点为4.0。报道了天然酶和还原酶的光谱特性。这种均一的酶还具有过氧化物酶和过氧化氢酶活性。
