Abstract
Publisher Summary This chapter describes an assay method and discusses the purification procedure for the enzyme Enzyme I from Salmonella typhimurium . The purification procedure involves precipitation with protamine sulfate, diethylaminoethyl (DEAE)-cellulose chromatography, precipitation with ammonium sulfate, gel filtration (AcA-44 Ultrogel), DEAE-Sephadex chromatography, and treatment with AcA-34. The purified Enzyme preparation is homogeneous when examined by polyacrylamide gel electrophoresis under native conditions and under denaturing conditions in sodium dodecyl sulfate. The monomeric subunit of Enzyme I has a molecular weight of about 58,000 as shown by the sedimentation equilibrium studies and from the gel filtration measurements under denaturing conditions. Enzyme I monomers undergo a reversible, temperature and concentration-dependent association. The optimum pH for Enzyme I activity is 7.2 in various buffer systems tested and Enzyme I is very sensitive to inhibition by sulfhydryl reagents and is relatively labile in the purified state.
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