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
This publication has 9 references indexed in Scilit:
- The Effect of Magnesium on Some Physical Properties of Yeast EnolaseJournal of Biological Chemistry, 1966
- Cooperative Effects in Binding by Bovine Serum Albumin. II. The Binding of 1-Anilino-8-naphthalenesulfonate. Polarization of the Ligand Fluorescence and Quenching of the Protein Fluorescence*Biochemistry, 1966
- Cooperative Effects in Binding by Bovine Serum Albumin. I. The Binding of 1-Anilino-8-naphthalenesulfonate. Fluorimetric Titrations*Biochemistry, 1966
- Hydrogen Ion Buffers for Biological Research*Biochemistry, 1966
- A Purification of Brewers' and Bakers' Yeast Enolase Yielding a Single Active ComponentJournal of Biological Chemistry, 1964
- Studies on Rabbit Muscle Enolase. Chemical Evidence for Two Polypeptide Chains in the Active Enzyme*Biochemistry, 1964
- Apparatus for rapid and sensitive spectrophotometryBiochemical Journal, 1964
- FRAGMENTATION OF BOVINE SERUM ALBUMIN BY PEPSIN .2. ISOLATION AMINO ACID COMPOSITION + PHYSICAL PROPERTIES OF FRAGMENTS1964
- Amino Acid Composition and Amino-Terminal Sequence of Yeast EnolaseJournal of Biological Chemistry, 1959