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An Analysis Of Protein-Ligand Interactions For Enzyme Ii-Mannitol From Escherichia Coli, Brent Lee Wood

Loma Linda University Electronic Theses, Dissertations & Projects

Enzyme II^mtl of Escherichia coli was purified from mtlA-overexpressing E. coli strain LJ1112 extraction of isolated membranes with deoxycholate, followed by hexyl agarose and ω-amino hexyl agarose chromatography in Lubrol PX. A 10-fold increase in total pure protein and 2.5-fold increase in specific activity over previously reported procedures was obtained. Tryptic fragments of Enzyme II^mtl were also purified and identified as the membrane and cytoplasmic domains by protein sequencing and SDS-PAGE. The fluorescence spectrum of Enzyme II^mtl suggested that two populations of tryptophan residues existed with emission maxima at 322 and 344 nm, corresponding to buried …