Purification and characterization of adenosine deaminase from Klebsiella sp. LF 1202

Abstract

Adenosine deaminase was induced when the cells of Klebsiella sp. LF 1202 were cultured in the medium containing adenosine as a sole source of carbon and nitrogen. The induction was partially repressed by the addition of ammonium sulfate in the medium. The amount of adenosine deaminase reached approximately 4.6% of the total intracellular soluble proteins. The enzyme was purified approximately 22-fold with a 25% activity yield. The enzyme was a monomer with a molecular weight of 26,000. The optimal activity was obtained at pH 8.0, 37°C, and the K m value for adenosine was 37 μM. Metal ions such as Zn 2+, Co 2+, Fe 2 and Ni + inhibited the activity of the enzyme. Sulfhydryl blocking agents such as p-chloromercuribenzoate and HgCl 2 were also found to be potent inhibitors for adenosine deaminase.