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J Bacteriol. 1969 April; 98(1): 69-74
Copyright © 1969 American Society for Microbiology. All Rights Reserved.
a Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305
ABSTRACT
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.
2 Present address: Laboratory of Molecular Biology, Hills Road, Cambridge, England.
1 The material in this paper is taken in part from a dissertation presented to the Graduate School of Stanford University by J. A. Spudich in partial fulfillment of the requirements for the Ph.D. degree.
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