@article {571011,
	title = {Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properites ♅},
	journal = {Eur J Biochem},
	volume = {59},
	number = {2},
	year = {1975},
	note = {notes},
	month = {1975 Nov 15},
	pages = {377-86},
	abstract = {Arginine decarboxylase which makes its appearance in Lathyrus sativus seedlings after 24 h of seed germination reaches its highest level around 5-7 days, the cotyledons containing about 60\% of the ♅ total activity in the seedlings at day 5. The cytosol enzyme was purified 977-fold from whole seedlings by steps involving manganese chloride treatment, ammonium sulphate and acetone fractionations, positive adsorption on alumina C-gamma gel, DEAE-Sephadex chromatography followed by preparative disc gel electrophoresis. The enzyme was shown to be homogeneous by electrophoretic and immunological criteria, had a molecular weight of 220,000 and appears to be a hexamer with identical subunits. The optimal pH and temperature for the enzyme activity were 8.5 and 45 degrees C respectively. The enzyme follows typical Michaelis-Menten kinetics with a Km value of 1.73 mM for arginine. Though Mn2+ at lower concentrations stimulated the enzyme activity, there was no dependence of the enzyme on any metal for the activity. The arginine decarboxylase of L. sativus is a sulfhydryl enzyme. The data on co-factor requirement, inhibition by carbonyl reagents, reducing agents and pyridoxal phosphate inhibitors, and a partial reversal by pyridoxal phosphate of inhibition by pyridoxal-HCl suggests that pyridoxal 5{\textquoteright}-phosphate is involved as a co-factor for the enzyme. The enzyme activity was inhibited competitively by various amines including the product agmatine. Highest inhibition was obtained with spermine and arcain. The substrate analogue, L-canavanine, homologue L-homoarginine and other basic amino acids like L-lysine and L-ornithine inhibited the enzyme activity competitively, homoarginine being the most effective in this respect.},
	keywords = {Amino Acids, Carboxy-Lyases, Cytosol, Drug Stability, Hydrogen-Ion Concentration, Immunodiffusion, Kinetics, Macromolecular Substances, Manganese, Molecular Weight, Plant Development, Plants, Pyridoxal Phosphate, Subcellular Fractions, Sulfhydryl Reagents, Temperature},
	issn = {0014-2956},
	url = {http://www.cambridge.org/isbn/1166158},
	author = {Ramakrishna, S and Adiga, P R}
}
