Begonia G B, Salin M L
Department of Biochemistry and Molecular Biology, Mississippi State University, Mississippi 39762.
J Bacteriol. 1991 Sep;173(17):5582-4. doi: 10.1128/jb.173.17.5582-5584.1991.
Exposure of Halobacterium halobium to 50 degrees C for 2.5 h in an aerobic environment resulted in a greater than twofold increase in the activity of the manganese-containing superoxide dismutase. Nondenaturing polyacrylamide gels stained for enzymatic activity did not reveal any additional isozymes of superoxide dismutase induced by the heat shock. The maximal effect was observed at 50 degrees C, and the elevated levels of activity remained constant during 5 h of recovery at 40 degrees C. The induction of enzymatic activity was sensitive to protein synthesis inhibitors. The results are discussed relative to heat shock and stress-related proteins as well as alterations in metabolism brought about by elevated temperatures.
在需氧环境中将嗜盐嗜盐杆菌暴露于50摄氏度2.5小时,导致含锰超氧化物歧化酶的活性增加两倍以上。对酶活性进行染色的非变性聚丙烯酰胺凝胶未显示热休克诱导的超氧化物歧化酶的任何其他同工酶。在50摄氏度时观察到最大效应,并且在40摄氏度恢复5小时期间活性升高水平保持恒定。酶活性的诱导对蛋白质合成抑制剂敏感。相对于热休克和应激相关蛋白以及温度升高引起的代谢变化,对结果进行了讨论。