Arginine Appears not to be Located in the Active Site of Na+/K+-ATPase

  • O. D. Lopina
  • M. Vachova

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.

Keywords

Hydrolysis Arginine Borate Butanedione Arginyl 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    De Pont JJHHM, Shoot BM, Van Proooijen AVE, Bonting SL (1977) An essential arginine residue in ATP-binding centre of (Na + K )-ATPase. Biochim Biophys Acta 482: 213–227PubMedGoogle Scholar
  2. 2.
    Grisham CM (1979) Characterization of essential arginyl residues in sheep kidney (Na+ + K+)-ATPase. Biochem Biophys Res Commun 88: 229–236.PubMedCrossRefGoogle Scholar
  3. 3.
    Lopina O, Skackova D, Baranova L, Khropov Yu (1991) Inhibition of Na,K-ATPase by new ATP analog, adenosine-5-N-(2,4-dinitro-5-fluorophenyl)phosphohydrazide. FEBS Lett 282: 228–230.PubMedCrossRefGoogle Scholar
  4. 4.
    Pedemonte CH, Kaplan JH (1988) Modification of arginine residues in the Na +,K+-ATPase. Biophys J 53: 222a.Google Scholar
  5. 5.
    Smith TW (1988) Purification of Na +,K+-ATPase from the supraorbital salt glands of the duck. Methods in Enzymol 156: 46–47.CrossRefGoogle Scholar

Copyright information

© Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt 1994

Authors and Affiliations

  • O. D. Lopina
    • 1
  • M. Vachova
    • 1
  1. 1.Department of Biochemistry, School of BiologyMoscow State UniversityMoscowRussia

Personalised recommendations