Structural studies on H+,K+-ATPase: determination of the NH2-terminal amino acid sequence and immunological cross-reactivity with Na+,K+-ATPase

Biochem Biophys Res Commun. 1986 Jul 16;138(1):185-92. doi: 10.1016/0006-291x(86)90264-0.

Abstract

The NH2-terminal amino acid sequence of the 100 kilodalton subunit of porcine gastric H+,K+-ATPase has been determined to be YKAENYELYQVELGPGP. Although the NH2-terminal region of this protein is not similar to the same region of the lamb kidney Na+,K+-ATPase catalytic subunit, other regions of these ATPase proteins appear to be homologous. Both monoclonal and polyclonal antibodies raised to lamb kidney Na+,K+-ATPase and its alpha, but not beta, subunit cross-react with the 100 kilodalton protein of H+,K+-ATPase.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Amino Acid Sequence
  • Animals
  • Cross Reactions
  • Electrophoresis, Polyacrylamide Gel
  • H(+)-K(+)-Exchanging ATPase
  • Kidney / enzymology
  • Macromolecular Substances
  • Molecular Weight
  • Sheep
  • Sodium-Potassium-Exchanging ATPase / immunology*
  • Structure-Activity Relationship

Substances

  • Macromolecular Substances
  • Adenosine Triphosphatases
  • H(+)-K(+)-Exchanging ATPase
  • Sodium-Potassium-Exchanging ATPase