Multiple forms of aspartate amino transferase from germinated green gram (Phaseolus aureus Roxb.).

L-Aspartate 2-oxoglutarate aminotransferases (EC 2.6.1.1), one from the supernatant and
three from the mitochondrial extract of 3-day old seedlings of green gram, have been purified and
some of their properties studied. The major supernatant enzyme (200-foid purified) moved as a
singie band of en~yme activity on polyacrylamide gel electrophoresis. All the partially purified
enzymes were anionic as shown by agar gel electrophoresis at pH 7·4. Kinetic studies indicated
a binary mechanism being operative. Data obtained on pH pattern, Km vaiues, eiectrophoretIc
and chromatographic studies· suggest isoenzymic nature of these enzyme forms.