Abstract
1. A method of stabilizing the enzyme by using glycerol is described. 2. A purification procedure is presented giving a higher purification than previously described. 3. Data showing substrate activation and activation by citrate are presented. 4. Kinetic constants for NAD+, NADH and certain bivalent metal ions are given. 5. Pronounced inhibitory buffer effects are described. 6. A brief comparison between the NAD-specific isocitrate dehydrogenase from peas and that from other sources is made.