Sharipova M R, Balaban N P, Mardanova A M, Nekhotyaeva N V, Dementyev A A, Vershinina O A, Garusov A V, Leshchinskaya I B
Department of Microbiology, School of Biology, Kazan State University, Kazan, 420008, Russia.
Biochemistry (Mosc). 1998 Oct;63(10):1178-82.
Alkaline phosphatase (APase) was isolated from the culture liquid of the streptomycin-resistant strain of Bacillus intermedius S3-19 and purified as a homogeneous preparation by ion-exchange chromatography and FPLC. Electrophoresis and gel-filtration revealed that the active enzyme is a monomer with molecular weight of 46-47 kD. The enzyme possessed phosphomonoesterase and phosphodiesterase activities with maximal levels at pH 9.5 and 55 degreesC and was stable until 60 degreesC at pH 8.0-10.0. The isolated APase exhibits a broad specificity towards a wide variety of substrates. The effect of divalent metal ions and other reagents on its catalytic activities was studied. It was concluded that alkaline phosphatase of B. intermedius is similar to the secreted alkaline phosphatases from other Bacillus species in its physicochemical and catalytic properties.
碱性磷酸酶（APase）从中间芽孢杆菌S3 - 19链霉素抗性菌株的培养液中分离出来，并通过离子交换色谱法和快速蛋白质液相色谱法（FPLC）纯化得到均一制剂。电泳和凝胶过滤显示，活性酶是一种分子量为46 - 47 kD的单体。该酶具有磷酸单酯酶和磷酸二酯酶活性，在pH 9.5和55℃时活性最高，在pH 8.0 - 10.0时，直到60℃都稳定。分离出的APase对多种底物表现出广泛的特异性。研究了二价金属离子和其他试剂对其催化活性的影响。得出的结论是，中间芽孢杆菌的碱性磷酸酶在物理化学和催化特性方面与其他芽孢杆菌属分泌的碱性磷酸酶相似。
