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- W2057122792 abstract "Transfer factor Tu has been purified to apparent homogeneity from extracts of Escherichia coli. Its molecular weight is about 42,000, and as routinely isolated the crystalline protein contains 1 mole of bound GDP. The bound nucleotide can be removed by dialysis of the protein in the absence of Mg2+. The protein contains a sulfhydryl group essential for GDP binding, which in Tu free of nucleotide reacts readily with N-ethylmaleimide, but in Tu-GDP is almost inert. The dissociation constant of Tu-GDP was determined to be 3 × 10−9m in 0.01 m MgCl2, pH 8, 20 °, and 8 × 10−6m in the absence of Mg2+. The dissociation constants of Tu-GTP and Tu-Ts were determined to be 3 × 10−7m and 2 × 10−9m, respectively, in 0.01 m Mg2+." @default.
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- W2057122792 title "Studies on the purification and properties of factor Tu from E. coli" @default.
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- W2057122792 doi "https://doi.org/10.1016/0003-9861(70)90102-5" @default.
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