NADP-dependent isocitrate dehydrogenase from the mussel Mytilus edulis L. 1. Purification and characterisation.
A purification scheme is described for NADP-dependent isocitrate dehydrogenase from the digestive gland of Mytilus edulis. The scheme incorporates three chromatographic steps: hydroxyapatite adsorption, blue-Sepharose affinity chromatography and DEAE-Sephacel ion-exchange chromatography. The subunit molecular weight of the enzyme was 45 000 (+/- 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.
D000818:Animals; D049872:Bivalvia / Q000201:enzymology*; D002846:Chromatography, Affinity; D004064:Digestive System / Q000201:enzymology; D007521:Isocitrate Dehydrogenase / Q000302:isolation & purification* / Q000378:metabolism; D046911:Macromolecular Substances; D008970:Molecular Weight; D009249:NADP
D046911:Macromolecular Substances; D009249:NADP; D007521:Isocitrate Dehydrogenase