Fatty acid composition of lipids which copurify with band 3.
In a previous study (L. R. Maneri and P. S. Low (1988) J. Biol. Chem. 263, 16170-16178) we determined that the anion transport protein, band 3, was significantly stabilized by lipids containing saturated and/or long chain fatty acids. To determine whether this thermodynamic preference is reflected in the composition of lipids tightly associating with the anion transporter in vivo, we have analyzed the fatty acid content of phospholipids co-isolating with the purified integral domain of band 3. Our data demonstrate that although stearic acid comprises only 14% of the bulk lipid fatty acids of the red cell membrane, it constitutes -68% of the fatty acids of lipids co-isolating with band 3. Certain other long chain fatty acids were also enriched in the adherent lipids. These results suggest that the fatty acids which most effectively stabilize band 3 also have the highest affinity for the transport protein.
Maneri
L R
LR
Department of Chemistry, Purdue University, West Lafayette, Indiana 47907.
Low
P S
PS
D001457:Anion Exchange Protein 1, Erythrocyte / Q000302:isolation & purification*; D005227:Fatty Acids / Q000032:analysis; D006801:Humans; D007700:Kinetics; D008563:Membrane Lipids / Q000097:blood* / Q000302:isolation & purification; D010743:Phospholipids / Q000097:blood* / Q000302:isolation & purification
D001457:Anion Exchange Protein 1, Erythrocyte; D005227:Fatty Acids; D008563:Membrane Lipids; D010743:Phospholipids