Abstract
Pyruvate kinase from M. expansa has been partially purified by ammonium sulphate fractionation. It exists in at least two forms. One form is precipitated at 40 per cent saturation, has a pH optimum of 6.5, is activated by fructose-1, 6-diphosphate, has a high affinity for Mn 2+ ions, and is inhibited by malate. The other form is precipitated at 50 per cent saturation, has a pH optimum of 7.0, is not activated by fructose-1, 6-diphosphate, and has a lower affinity for Mn 2+ ions. Malate inhibition in the 40 per cent fraction is due to competition with phospho-enol-pyruvate. The relevance of these findings to metabolic regulation in the tapeworm is discussed.
Published Version
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