Characterization of the enolase isozymes of rabbit brain: kinetic differences between mammalian and yeast enolases
| Autor: | Abbey Klugerman, Mary Judith Kornblatt |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Enolase
Kinetics Saccharomyces cerevisiae Biology Biochemistry Isozyme Divalent Animals Magnesium Molecular Biology Mammals chemistry.chemical_classification Phosphoglycerate kinase Brain Cell Biology Cations Monovalent Rabbit brain Molecular biology Yeast Molecular Weight chemistry Phosphopyruvate Hydratase Rabbits Phosphoenolpyruvate carboxykinase |
| Zdroj: | Biochemistry and Cell Biology. 67:103-107 |
| ISSN: | 1208-6002 0829-8211 |
| DOI: | 10.1139/o89-016 |
| Popis: | Two isozymes of enolase, αα and γγ, have been purified from rabbit brain and characterized. The kinetic properties of αα and γγ (pH optimum, Km for phosphoglycerate and phosphoenolpyruvate, requirement for a divalent cation) are very similar to those of rabbit enolase, form ββ, and to those of enolase isozymes from other species. However, several novel properties were observed. (i) All the enolases studied were inhibited by Na+ and Li+. (ii) The rabbit enolases, but not yeast enolase, were activated by K+, NH4+, Cs+, and Rb+. (iii) Rabbit enolase is more susceptible to inhibition by excess Mg2+ than is the yeast enolase; the increased inhibition by Mg2+ above pH 7.1 accounts, at least in part, for the observed differences between mammalian and yeast enolases in their pH optima for activity.Key words: enolase, isozymes, kinetics. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|