Abstract
Two α-dicarbonyl reagents, phenylglyoxal and 2,3-butanedione, were used to demonstrate the presence of essential arginine residues in the mechanism of the plasma membrane Ca 2+-ATPase of red beet ( Beta vulgaris L.) storage tissue. Both the ATP-dependent 45Ca 2+ transport and ITP hydrolytic activities of the Ca 2+-ATPase were inhibited by these reagents. Optimal inhibition was observed at pH 7.5 and 25°. Inhibition of ATP dependent 45Ca 2+ transport by phenylglyoxal and 2,3-butanedione was decreased by inclusion of ATP in the incubation medium. These results demonstrate that arginine residues are involved in the mechanism of the red beet plasma membrane Ca 2+-ATPase and may reside at the ATP binding region of the enzyme active site.
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