Phosphorylation of glycophorin A in membranes of intact human erythrocytes.
The qualitative and quantitative contribution of glycophorin A phosphorylation to the general and specific pattern of membrane protein phosphorylation in intact erythrocytes pre-incubated with 32Pi was examined. Intense 32P-labeled bands at 88,000 and 38,000 Mr were identified as phosphorylated glycophorin A dimer and monomer respectively on the basis of several criteria. Quantitatively, phosphorylated glycophorin A dimer accounted for about 70% of 32P in the band 3 region. This value is at least three times that previously reported. The results of ancillary experiments involving selective extraction of ghosts in acidified chloroform/methanol solvents and electrophoresis in the presence of detergents make it unlikely that the 32P associated with glycophorin A was due to bound polyphosphoinositides.
Dzandu
J K
JK
Deh
M E
ME
Kiener
P
P
D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism*; D006021:Glycophorins / Q000378:metabolism*; D006801:Humans; D046911:Macromolecular Substances; D009439:Neuraminidase / Q000494:pharmacology; D010750:Phosphoproteins / Q000097:blood*; D010766:Phosphorylation; D012795:Sialoglycoproteins / Q000097:blood / Q000378:metabolism*; D012834:Silver; D013194:Staining and Labeling
D006021:Glycophorins; D046911:Macromolecular Substances; D010750:Phosphoproteins; D012795:Sialoglycoproteins; D012834:Silver; D009439:Neuraminidase