Structural studies on H+,K+-ATPase: determination of the NH2-terminal amino acid sequence and immunological cross-reactivity with Na+,K+-ATPase.
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.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D017506:H(+)-K(+)-Exchanging ATPase; D007668:Kidney / Q000201:enzymology; D046911:Macromolecular Substances; D008970:Molecular Weight; D012756:Sheep; D000254:Sodium-Potassium-Exchanging ATPase / Q000276:immunology*; D013329:Structure-Activity Relationship
D046911:Macromolecular Substances; D000251:Adenosine Triphosphatases; D017506:H(+)-K(+)-Exchanging ATPase; D000254:Sodium-Potassium-Exchanging ATPase