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. 1988 May;87(1):126–129. doi: 10.1104/pp.87.1.126

Essential Arginyl Residues in the Plasma Membrane H+-ATPase from Vigna radiata L. (Mung Bean) Roots 1

Kunihiro Kasamo 1
PMCID: PMC1054710  PMID: 16666087

Abstract

Proton-translocating ATPase (H+-ATPase) was purified from mung bean (Vigna radiata L.) roots. Treatment of this enzyme with the arginine-specific reagent 2,3-butanedione in the presence of borate at 37°C (pH 7.0), caused a marked decrease in its activity. Under this condition, half-maximal inhibition was brought about by 20 millimolar 2,3-butanedione at 12 minutes. MgATP and MgADP, the physiological substrate and competitive inhibitor of the ATPase, respectively, provided partial protection against inactivation. Loss of activity followed pseudo-first order kinetics with respect to 2,3-butanedione concentration, and double log plots of pseudo-first order rate constants versus reagent concentration gave a curve with a slope of 0.984. Thus, inactivation may possibly result from reaction of one arginine residue at each active site of the enzyme. The results obtained from the present study indicate that at least one arginyl residue performs an essential function in the plasma membrane H+-ATPase, probably at the catalytic site.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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