Yeast enolase carboxyl modification using Woodward's reagent K
Keyword(s):
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.
1985 ◽
Vol 50
(2)
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pp. 445-453
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1981 ◽
Vol 11
(3)
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pp. 209-254
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2019 ◽
Vol 8
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pp. 93-100
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2008 ◽
Vol 2008
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pp. 1-10
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1983 ◽
Vol 19
(3)
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pp. 255-267
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1985 ◽
Vol 24
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pp. 47-57
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1981 ◽
Vol 61
(2)
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pp. 469-474
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