The (Na+, K+)ATPase exhibits enzymic activity in the absence of the glycoprotein subunit.
Membrane-bound (Na+, K+)ATPase from avian nasal salt glands was exposed to limited papain digestion. Such treatment results in the selective removal of the beta-subunit rendering the alpha-subunit still membrane-bound and expressing full enzymic activity. With further exposure to papain the alpha-chain becomes fragmented into two major polypeptide components. The fragmented membrane-bound catalytic chain is extremely sensitive to detergent treatment and cannot be solubilized in an active state.
D000818:Animals; D001717:Birds; D003902:Detergents; D006023:Glycoproteins / Q000378:metabolism*; D046911:Macromolecular Substances; D010206:Papain / Q000378:metabolism; D012491:Salt Gland / Q000201:enzymology; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D012995:Solubility
D003902:Detergents; D006023:Glycoproteins; D046911:Macromolecular Substances; D010206:Papain; D000254:Sodium-Potassium-Exchanging ATPase