Arginine Appears not to be Located in the Active Site of Na+/K+-ATPase
O. D. Lopina, Mariana Vachová
Abstract
O. D. Lopina, Mariana Vachová
Abstract
It was found that modification of Na + /K + -ATPase by arginine specific reagents produced inhibition of the enzyme activity (1,2,4). ATP (1,2,4) and ADP (1,2) protected Na + /K + -ATPase against the inactivation. These data supported the idea that an arginine residue is located in nucleotide binding site of Na + /K + ATPase. We have compared inhibition of Na + K + ATPase from duck salt gland by two arginine specific reagents 2,3-butanedione and phenylglyoxal in the presence of three essential ligands — Na + , K + and ATP. These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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It was found that modification of Na + /K + -ATPase by arginine specific reagents produced inhibition of the enzyme activity (1,2,4). ATP (1,2,4) and ADP (1,2) protected Na + /K + -ATPase against the inactivation. These data supported the idea that an arginine residue is located in nucleotide binding site of Na + /K + ATPase. We have compared inhibition of Na + K + ATPase from duck salt gland by two arginine specific reagents 2,3-butanedione and phenylglyoxal in the presence of three essential ligands — Na + , K + and ATP. These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
Key concepts: Phenylglyoxal, Arginine, ATPase, Chemistry, Enzyme, Binding site, Reagent, Biochemistry