1Biometry Research Unit, Indian Statistical Institute, 203, B T Road, Calcutta 700 035, India
2Department of Botany and Centre for Plant Molecular Biology, Bose Institute, 93/1, A P C Road, Calcutta 700 009, India
* Corresponding author
Arginine decarboxylase (EC 4.1.1.19) has been purified and characterized from Brassica campestris cv B-9. The enzyme was purified 1120 fold and the recovery was 9%. The mol wt of the enzyme determined by gel filtration was 240 kD with identical subunits of 60 kD. The pH and temperature optima for the enzyme were 8.0 and 30°C respectively. The Km was 0.31 mM. Polyamines inhibited the enzyme activity significantly. Immunodiffusion with ADC-specific antibodies showed cross reactivity against purified ADC from Brassica.
polyamine, arginine decarboxylase, Brassica campestris
