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- W2020223818 abstract "Yeast enolase is inactivated by Woodward's reagent K. Substantial protection is afforded by binding of 1 mol of conformational metal ion/subunit. Inactivation is correlated with modification of 13 carboxyl groups/subunit in the absence of conformational metal ion and 17 in its presence. Ten tryptic peptides labeled by Woodward's reagent K can be isolated, mostly from the C-terminal half of the protein. The changes in reactivity of these peptides produced by conformational metal ion suggest direct coordination to Glu-181 together with a contraction of the protein." @default.
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- W2020223818 modified "2023-09-26" @default.
- W2020223818 title "Yeast enolase carboxyl modification using Woodward's reagent K" @default.
- W2020223818 cites W2252280792 @default.
- W2020223818 doi "https://doi.org/10.1139/o86-129" @default.
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