Partial covalent labeling with pyridoxal 5'-phosphate induces bis(sulfosuccinimidyl)suberate crosslinking of band 3 protein tetramers in intact human red blood cells.
Partial covalent labeling of band 3 protein lysines with pyridoxal 5'-phosphate (a substrate and affinity probe) changes the bis(sulfosuccinimidyl)suberate crosslinking pattern of band 3 in intact red cells from a mixture of dimers and tetramers to all tetramers as the exclusive crosslinked product. This is the first demonstration of band 3 crosslinkage to the tetrameric level within membranes of intact red cells. The possible implications of the ligand-induced change in the band 3 crosslinking pattern are discussed.
Salhany
J M
JM
Veterans Administration Medical Center, Omaha, Nebraska.
Sloan
R L
RL
D000345:Affinity Labels; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism*; D003432:Cross-Linking Reagents; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D011485:Protein Binding; D011732:Pyridoxal Phosphate / Q000378:metabolism / Q000494:pharmacology*; D013388:Succinimides / Q000378:metabolism*
D000345:Affinity Labels; D001457:Anion Exchange Protein 1, Erythrocyte; D003432:Cross-Linking Reagents; D013388:Succinimides; D011732:Pyridoxal Phosphate; C035760:bis(sulfosuccinimidyl)suberate