PMID: 1252Nov 15, 1975

Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properites

European Journal of Biochemistry
S Ramakrishna, P R Adiga

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 phosphat...Continue Reading

References

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Related Concepts

Carboxy-Lyases
Cytoplasmic Matrix
Drug Stability
Immunodiffusion Measurement
Hydrogen-Ion Concentration
Manganese
Pyridoxal Phosphate
Subcellular Fractions
Sulfhydryl Reagents
Plant Development

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