KEYNAN A, EVANCHIK Z, HALVORSON H O, HASTINGS J W
J Bacteriol. 1964 Aug;88(2):313-8. doi: 10.1128/jb.88.2.313-318.1964.
A. Keynan (Israel Institute of Biological Research, Ness Ziona, Israel), Z. Evenchik, H. O. Halvorson, and J. W. Hastings. Studies on the activation of bacterial endospores. J. Bacteriol. 88:313-318. 1964.-Heat activation of bacterial endospores was imitated by suspending spores in reducing agents (mercaptoethanol or thioglycolate) or in a pH less than 4.5. Urea (6 m) had no effect on spores. In addition to the well-known activation at 65 C for 45 min, spores were also activated by exposure to 34 C for 48 hr. The activation by heat and by reducing agents was reversible; the reverse reaction was temperature-dependent. No reversion occurred at -20 C, whereas at 28 C the spores reversed to their original dormant state within 72 hr. It is suggested that the heat-activation phenomenon could be explained by assuming that heat or reducing agents change the tertiary structure of a protein responsible for the maintenance of the dormant state by reducing the disulfide linkages which stabilize the protein in a specific configuration. The partial denaturation of this protein is reversible by reoxidation of the reduced disulfide bonds.
A.凯南(以色列生物研究所,内斯锡安纳,以色列)、Z.埃文奇克、H.O.哈尔沃森和J.W.黑斯廷斯。细菌芽孢激活的研究。《细菌学杂志》88:313 - 318。1964年。——通过将芽孢悬浮于还原剂(巯基乙醇或硫代乙醇酸盐)中或pH值小于4.5的环境中模拟细菌芽孢的热激活。6摩尔尿素对芽孢无影响。除了在65℃下45分钟这一广为人知的激活方式外,芽孢经34℃处理48小时也会被激活。热激活和还原剂激活是可逆的;逆反应取决于温度。在 - 20℃时不发生逆转,而在28℃时,芽孢在72小时内恢复到其原始休眠状态。有人提出,热激活现象可以这样解释:热或还原剂通过减少稳定蛋白质特定构型的二硫键,改变负责维持休眠状态的蛋白质的三级结构。这种蛋白质的部分变性可通过还原的二硫键的再氧化而逆转。