Properties of partially purified leaf ornithine aminotransferase of Brassica juncea under salt stress

Authors
Madan, S Nainawatee, HS
Citation
S. Madan et Hs. Nainawatee, Properties of partially purified leaf ornithine aminotransferase of Brassica juncea under salt stress, ACT PHYS PL, 22(4), 2000, pp. 445-450
Citations number
27
Categorie Soggetti
Plant Sciences
Journal title
ACTA PHYSIOLOGIAE PLANTARUM
ISSN journal
01375881 → ACNP
Volume
22
Issue
4
Year of publication
2000
Pages
445 - 450
Database
ISI
SICI code
0137-5881(2000)22:4<445:POPPLO>2.0.ZU;2-Z
Abstract
Properties of the partially purified L-ornithine: 2-oxoacid aminotransferas e (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 SR 3P6-2 was relatively more efficient in terms of its Km, Vmax, and Ea (activ ation energy) and required higher levels of chlorides for inhibition as com pared to the enzyme from the parent cv. Prakash. These results suggest some salt-stress related changes in the enzyme.