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Literature summary for 7.2.2.19 extracted from

  • Chow, D.C.; Forte, J.G.
    Characterization of the beta-subunit of the H+-K+-ATPase using an inhibitory monoclonal antibody (1993), Am. J. Physiol., 265, 1562-1570.
    View publication on PubMed
Search for more literature for 7.2.2.19

Inhibitors

Inhibitors Comment Organism Structure
antibody 2G11
-
 Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Oryctolagus cuniculus
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
95000
-
 x * 95000, alpha, + x * 60000-80000, beta, SDS-PAGE Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the beta-subunit is synthesized as a 52000 Da glycoprotein with seven N-linked precursor high-mannose oligosaccharides that mature into complex oligosaccharides Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
stomach
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in + K+/out
-
 Oryctolagus cuniculus ADP + phosphate + H+/out + K+/in
-
 ?

Subunits

Subunits Comment Organism
? x * 95000, alpha, + x * 60000-80000, beta, SDS-PAGE Oryctolagus cuniculus
More functional role of the beta-subunit in the H+-K+-ATPase activity especially the K+-induced conformational states Oryctolagus cuniculus