Abstract
A purification scheme is described for NADP-dependent isocitrate dehydrogenase from the digestive gland of M. edulis. The scheme incorporates 3 chromatographic steps: hydroxyapatite adsorption, blue-Sepharose affinity chromatography and DEAE-Sephacel ion-exchange chromatography. The subunit MW of the enzyme was 45000 (.+-. 5000) by sodium dodecylsulfate gel electrophoresis. The purified enzyme was homogeneous on dodecylsulfate gels and had a specific activity of 30-50 U/mg protein.