Concanavalin A binding to oligosaccharide chain leads to alterations in properties of band 3.
Anion transport activity and thermotropic behavior of Band 3 are found to be altered after binding of concanavalin (Con A) to human erythrocyte ghosts and isolated Band 3. At lower Con A concentration, the rate coefficients of anion transport enhance with increasing Con A concentration, while noticeable changes of the largest calorimetric endotherm of human erythrocyte membranes termed the C transition (Band 3) can not be observed. With 50 micrograms/ml of Con A, the rate coefficient of Con A-modified ghosts increases 34.4% in comparison with that of normal ghosts. Binding of Con A in lower concentration to ghosts bring about increase of fluidity of lipid which maybe contribute to increase anion transport via Band 3. At higher Con A concentration, the C transition tend to lower temperature with increase in Con A concentration, the C transition is shifted from 69.25 degrees C to 66.25 degrees C with 2.5 mg/ml Con A. It is suggested that the Con A-modified Band 3 possess a looser structure than normal one.
Zhang
Z G
ZG
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
Lu
J Z
JZ
Chen
J W
JW
D001457:Anion Exchange Protein 1, Erythrocyte / Q000737:chemistry / Q000378:metabolism*; D000838:Anions / Q000378:metabolism; D001692:Biological Transport; D002152:Calorimetry, Differential Scanning; D003208:Concanavalin A / Q000494:pharmacology*; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000378:metabolism; D005454:Fluorescence Polarization; D006801:Humans; D008562:Membrane Glycoproteins / Q000737:chemistry; D009844:Oligosaccharides / Q000737:chemistry; D013696:Temperature
D001457:Anion Exchange Protein 1, Erythrocyte; D000838:Anions; D008562:Membrane Glycoproteins; D009844:Oligosaccharides; D003208:Concanavalin A