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- W1573162261 abstract "The malK gene, encoding a membrane-associated component of the maltose transport complex of Salmonella typhimurium was cloned into an expression vector downstream of the promoters lambda pR and lambda pL and a strong translation initiation region. Escherichia coli strain JM109 harboring the resulting plasmid pCW14 synthesized a protein of apparent molecular mass of 43 kDa upon temperature shift, as demonstrated by sodium dodecyl sulfate-gel electrophoresis. The identity of the protein was determined by N-terminal amino acid sequencing. The overproduced protein was sequestered in inclusion bodies as revealed by electron microscopy. The protein was purified to homogeneity on a large scale by disrupting the cells with a passage through a Ribi press, solubilizing the inclusion bodies with urea, and subsequent chromatography on Red Agarose. Purified MalK, as the membrane-bound MalK protein could be covalently modified by [gamma-32P]8-azido-ATP. Furthermore, the purified protein bound [gamma-32P] ATP with a dissociation constant of 150 microM and exhibited ATPase activity, which was stimulated by dimethyl-sulfoxide and inhibited by ADP." @default.
- W1573162261 created "2016-06-24" @default.
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- W1573162261 date "1992-05-01" @default.
- W1573162261 modified "2023-10-13" @default.
- W1573162261 title "Large scale purification, nucleotide binding properties, and ATPase activity of the MalK subunit of Salmonella typhimurium maltose transport complex." @default.
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- W1573162261 doi "https://doi.org/10.1016/s0021-9258(19)50360-x" @default.
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