Smith L A, Chirikjian J G
J Biol Chem. 1979 Feb 25;254(4):1003-6.
The specific endonuclease Bam HI from Bacillus amyloliquefaciens (RUB 500) has been purified to apparent homogeneity. Two active forms of the enzyme corresponding to the dimeric and tetrameric forms have been isolated. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the enzyme dissociated into Mr = 22,000 +/- 500 subunits. Bam HI has a broad pH optimum on the alkaline side and requires Mg2+ which can be partially replaced by Mn2+. The enzyme catalysis appears to be governed by a two-step mechanism.
来自解淀粉芽孢杆菌（RUB 500）的特异性内切核酸酶Bam HI已被纯化至表观均一。已分离出该酶的两种对应于二聚体和四聚体形式的活性形式。在十二烷基硫酸钠-聚丙烯酰胺凝胶电泳上，该酶解离成Mr = 22,000 ± 500的亚基。Bam HI在碱性侧有较宽的最适pH值，需要Mg2+，Mg2+可部分被Mn2+取代。该酶的催化作用似乎受两步机制支配。
