Abstract
A study of some properties of L-glutamate dehydrogenase (GDH) in the supernatant and mitochondrial fractions of mung bean hypocotyls failed to reveal any differences between the two enzymes. GDH in lettuce leaf chloroplasts was solubilized with Triton-X-100 and marked differences in a number of properties were found between this enzyme and the one solubilized from lettuce leaf mitochondria. It was concluded that the mitochondrial and chloroplastic GDH's are distinct enzymes. The small amount of GDH activity detected in isolated lettuce leaf peroxisomes could have been due to adsorption of the enzyme.
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