Covalent binding of negatively charged phospholipid to Na,K-ATPase.
Phosphatidylglycolaldehyde and its lyso derivative were applied as probes in order to study lipid-protein interactions with purified, membrane-bound Na,K-ATPase. Reduction with [3H]NaCNBH3 led to formation of a stable chemical derivative between added lipid and protein. The extent of modification of the two subunits of Na,K-ATPase was similar. Extensive tryptic digestion of derivatized ATPase resulted in cleavage of the alpha-subunit without hydrolysis of the beta-subunit.
D000818:Animals; D007425:Intracellular Membranes / Q000201:enzymology; D007679:Kidney Medulla / Q000201:enzymology; D008861:Microsomes / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis; D010713:Phosphatidylcholines / Q000378:metabolism*; D011485:Protein Binding; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*; D013552:Swine; D014357:Trypsin
D010446:Peptide Fragments; D010713:Phosphatidylcholines; D014357:Trypsin; D000254:Sodium-Potassium-Exchanging ATPase