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. 1982 Sep;38(3):261-6.

Partial purification and properties of mevalonate kinase from neonatal chick liver

J García-Martínez, A Linares, M D Suárez, E García-Peregrín
  • PMID: 6296930

Partial purification and properties of mevalonate kinase from neonatal chick liver

J García-Martínez et al. Rev Esp Fisiol. 1982 Sep.

Abstract

Mevalonate kinase from neonatal chick liver has been partially purified by ammonium sulphate precipitation and Sephadex G100 and DEAE-cellulose fractionation. The kinetic characteristics agreed with the sequential mechanism suggested for the enzyme and provided apparent Km values of 0.01 mM for mevalonic acid and 0.25 mM for ATP. Partially purified mevalonate kinase from neonatal chick liver showed an absolute specificity for ATP. Mn2+ was a better activator than Mg2+ at low concentrations (0.1-1.0 mM). Higher Mn2+ concentrations produced a clear inhibition of mevalonate kinase. Likewise, addition of EDTA, with or without metal ions, clearly inhibited the enzymatic reaction.

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