Spudich J A, Kornberg A
J Bacteriol. 1969 Apr;98(1):69-74. doi: 10.1128/jb.98.1.69-74.1969.
The spore and vegetative cell adenylate kinases of Bacillus subtilis, purified about 1,000-fold, proved indistinguishable by several physical and functional tests, including polyacrylamide gel electrophoresis, DEAE cellulose chromatography, and specificity toward substrates. Adenylate kinase activity in cell extracts, followed throughout growth and sporulation, was found to reach a maximum near the end of exponential growth, remain at that level during sporulation, until shortly before the appearance of refractile forms, and then decline, along with total protein, during the subsequent maturation of the spores. The enzyme, stable in extracts of exponential growing cells, was unstable in extracts of sporulating cells, presumably as a result of degradation by protease(s) appearing after the end of exponential growth.
枯草芽孢杆菌的孢子和营养细胞腺苷酸激酶经过约1000倍的纯化，通过包括聚丙烯酰胺凝胶电泳、DEAE纤维素色谱分析以及对底物的特异性等多项物理和功能测试，结果显示二者无法区分。在整个生长和孢子形成过程中跟踪细胞提取物中的腺苷酸激酶活性，发现其在指数生长末期附近达到最大值，在孢子形成期间保持在该水平，直到折射形态出现前不久，然后随着孢子随后的成熟，与总蛋白一起下降。该酶在指数生长细胞的提取物中稳定，但在孢子形成细胞的提取物中不稳定，推测这是指数生长结束后出现的蛋白酶降解的结果。
