Detailed structural analysis of exposed domains of membrane-bound Na+,K+-ATPase. A model of transmembrane arrangement.
Exposed regions of the alpha- and beta-subunits of membrane-bound Na+,K+-ATPase were in turn hydrolyzed with trypsin. Resistance of the beta-subunit to proteolysis was shown to be due mainly to the presence of disulfide bridge(s) in the molecule. A model for the spatial organisation of the enzyme in the membrane was proposed on the basis of detailed structural analysis of extramembrane regions of both subunits.
D000595:Amino Acid Sequence; D000818:Animals; D006868:Hydrolysis; D008565:Membrane Proteins / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D013552:Swine; D014357:Trypsin / Q000378:metabolism
D008565:Membrane Proteins; D014357:Trypsin; D000254:Sodium-Potassium-Exchanging ATPase