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- W1515591027 abstract "Abstract Factor IIIlac, a soluble, lactose-specific phosphocarrier protein of the Staphylococcus aureus phosphotransferase system, was purified to homogeneity. The molecular weight of the native protein was 35,000 as determined by both high and low speed equilibrium sedimentation. In concentrated guanidinium hydrochloride solutions the molecular weight as determined by similar methods as well as by analytical gel filtration was about 12,000. The results of amino acid analysis, radioactive labeling of sulfhydryl groups, and partial amino acid sequence determination were all consistent with the conclusion that Factor IIIlac contains three identical subunits. An analysis of the circular dichroic spectrum indicated that an unusually large amount of α helical structure (about 60%) was present. As shown in the succeeding paper in this series, phospho-Factor IIIlac is an intermediate in the lactose-phosphotransferase reaction sequence. Phosphorylation experiments under a wide range of conditions indicated that up to three phosphoryl groups could be transferred to Factor IIIlac, consistent with its trimeric structure. The chemical nature of phospho-Factor IIIlac was studied by several techniques. The rates of hydrolysis under different conditions, and chromatographic studies of the phosphohistidine obtained from an alkaline hydrolysate of the phospho-Factor IIIlac indicated that the three phosphoryl groups were linked to position N-3 in the imidazole ring of histidine residues." @default.
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- W1515591027 date "1973-02-01" @default.
- W1515591027 modified "2023-10-06" @default.
- W1515591027 title "Sugar Transport" @default.
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- W1515591027 doi "https://doi.org/10.1016/s0021-9258(19)44356-1" @default.
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