阴离子去污剂对嗜热细菌PS3分离出的F1的ATP酶活性的影响。

The effect of anionic detergents on the ATPase activity of isolated F1 from the thermophilic bacterium PS3.

作者信息

Norling B

出版信息

Biochem Biophys Res Commun. 1986 May 14;136(3):899-905. doi: 10.1016/0006-291x(86)90417-1.

Abstract

The ATPase activity of F1 isolated from the thermophilic bacterium PS3 is stimulated at 30 degrees C by the anionic detergents cholate or deoxycholate. Maximal activity obtained with these detergents (35 mumol/min X mg) is similar to the activity reported for the optimal temperature, 75 degrees C. The activity is linearly stimulated by the detergents and maximal activity is obtained at the critical micellar concentration of the respective detergent. The results are discussed in relation to the role of subunit interactions of the oligomeric enzyme during catalysis and the mode of interaction between the subunits.

摘要

从嗜热细菌PS3中分离出的F1的ATP酶活性在30℃时受到阴离子去污剂胆酸盐或脱氧胆酸盐的刺激。用这些去污剂获得的最大活性（35 μmol/分钟×毫克）与报道的75℃最佳温度下的活性相似。去污剂可线性刺激该活性，且在各自去污剂的临界胶束浓度下可获得最大活性。结合寡聚酶亚基相互作用在催化过程中的作用以及亚基之间的相互作用模式对结果进行了讨论。