Higuti I H, Stencel M, Nascimento K H, Nascimento A J
Departamento de Bioquímica, Universidade Federal do Paraná, Curitiba, PR., Brazil.
Cell Biochem Funct. 1992 Dec;10(4):237-41. doi: 10.1002/cbf.290100405.
The membrane ATPase (EC 3.6.1.3) of Bacillus cereus was solubilized by a 'shock-wash' process and purified. The non-specific phosphatase contaminant was separated by glycerol density gradient centrifugation. The optimum temperature was 39.5 degrees C and the pH optimum at 7.5. On SDS-polyacrylamide gel electrophoresis two classes of subunits were observed in equal proportions with molecular weights of 70 K and 83 K. The effect of various compounds on the enzymatic activity was studied. The enzyme was insensitive to NaN3, oligomycin and to divalent cations, but was inhibited by citrate and oxalate.
蜡样芽孢杆菌的膜ATP酶（EC 3.6.1.3）通过“休克洗涤”过程溶解并纯化。非特异性磷酸酶污染物通过甘油密度梯度离心分离。最适温度为39.5℃，最适pH为7.5。在SDS-聚丙烯酰胺凝胶电泳上观察到两类亚基，比例相等，分子量分别为70K和83K。研究了各种化合物对酶活性的影响。该酶对叠氮化钠、寡霉素和二价阳离子不敏感，但受柠檬酸盐和草酸盐抑制。
