Abstract
Glutamate decarboxylase (GAD) was purified 300-fold from green cowpea ( Vigna unguiculata L.) pods using a combination of PEG precipitation, DEAE cellulose chromatography, hydroxylapatite chromatography, and Q-resin chromatography. The partially purified preparation demonstrated 2 primary bands in SDS-polyacrylamide gel electrophoresis with up to 3 additional minor bands. Cowpea GAD has a pH optimum at between pH 5.5–6.0, and an apparent K M for glutamate of 3.2 mM at pH 5.8. Both crude GAD preparations and preparations partially purified through the hydroxylapatite step can be stimulated by Ca 2+ and calmodulin when assayed at pH 5.8. However, the purified enzyme does not show activation by Ca 2+ and/or calmodulin at pH 5.8 or at pH 7.0. © 1997 Elsevier Science Ltd. All rights reserved
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