Abstract
Pyruvate-dependent 4-aminobutyrate transaminase (EC 2.6.1.19) activity in crude extracts or lysed mitochondrial preparations from tobacco (Nicotiana tabacum L. cv Samsun N.N.) leaf was separated from 2-oxoglutarate-dependent GABA-T activity by FPLC anion exchange chromatography. Pyruvate-dependent GABA-T was partially purified 1530-fold by a combination of mitochondrial isolation and FPLC anion-exchange chromatography. This enzyme preparation had an apparent Km of 1.220.2 mM for GABA and 0.2420.05 mM for pyruvate. Two-oxoglutarate-dependent GABA-T activity was not detected in the partially purified preparation. Our data indicate the existence of a pyruvate-specific mitochondrial GABA-T. # 1999 Elsevier Science Ltd. All rights reserved.
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