The reversible dissocation of yeast enolase.
Open Access
- 1 January 1968
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 59 (1) , 216-223
- https://doi.org/10.1073/pnas.59.1.216
Abstract
Yeast enolase consists of 2 inactive subunits of approximately 34,000 molecular weight. High concentrations of potassium chloride facilitate dissociation, though equivalent concentrations of potassium acetate do not. Mg ion lowers the subunit dissociation constant. From the kinetics of recovery of activity and the fluorescence changes occurring upon addition of Mg to enzyme in 1 M potassium chloride, it is concluded that one mole of Mg combines with one subunit, producing some change in the half-molecule which increases its affinity for the other subunit.Keywords
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