PMID:6311616

Citation	Bârzu, O and Michelson, S (1983) Simple and fast purification of Escherichia coli adenylate kinase. FEBS Lett. 153:280-4
Abstract	Adenylate kinase from E. coli (strains CR341 and CR341 T28, a temperature-sensitive mutant) was purified by a two-step chromatographic procedure. The enzyme from crude extracts of both mutant and parent strain was bound to blue-Sepharose at pH 7.5, thereafter specifically eluted with 0.05 mM P1,P5-di(adenosine-5')pentaphosphate. A second chromatography on Sephadex G-100 yielded pure enzyme. E. coli adenylate kinase was strongly inhibited by P1,P5-di(adenosine-5')pentaphosphate (Ki 0.6 microM for adenylate kinase of strain CR341 and 2.1 microM in the case of mutant enzyme). After denaturation in 6 M guanidinium hydrochloride both mutant and parent adenylate kinase returned rapidly to the native, active state by dilution of guanidinium hydrochloride.
Links	PubMed
Keywords	Adenylate Kinase/isolation & purification; Adenylate Kinase/metabolism; Escherichia coli/enzymology; Kinetics; Macromolecular Substances; Molecular Weight; Mutation; Phosphotransferases/isolation & purification; Temperature
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