Abstract
Properties of the partially purified L-ornithine: 2-oxoacid aminotransferase (EC 2.6.1.13) of leaves of Brassica juncea salt tolerant somaclone SR3P6-2 and its parent cv. Prakash were studied. The enzyme from the somaclone SR3P6-2 was relatively more efficient in terms of its Km, Vmax, and Ea (activation energy) and required higher levels of chlorides for inhibition as compared to the enzyme from the parent cv. Prakash. These results suggest some salt-stress related changes in the enzyme.
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