Anion exchange band 3 protein

The major proteins (which include spectrin, ankyrin, the anion exchange protein, actin, and band 4.1) have been studied intensively, and the principal features of their disposition (eg, integral or peripheral), structure, and function have been established. 

The anion exchange protein (band 3) is a transmembrane glycoprotein, with its carboxyl terminal end on the external surface of the membrane and its amino terminal end on the cytoplasmic surface. It is an example of a multipass membrane protein, extending across the... 

In common with M. macedonicus, urine from male M. spretus also demonstrated a MUP-sized band following gel electrophoresis. The proteins within this band were analysed by high resolution anion exchange chromatography and electrospray ionisation mass spectrometry (ESI-MS). The former technique produced an elution profile consisting of just three peaks, in contrast to both the more complex patterns observed previously from M. m. domesticus and the single major peak in M. macedonicus. Furthermore, similar analyses from five individual males resulted in near... 

Band 3 Anion exchanger 95 K I Anion transport binding sites for ankyrin, protein 4.2... 

Hereditary spherocytosis is a common human inherited hemolytic anemia caused by mutations in erythrocyte anion exchanger type 1 known also as Band 3 protein. The substitution of the highly conserved Met663 to positively charged Lys located in the extracellular boundary of TM8 was recently described in a patient with the disease (Lima et al., 2005). This novel Band 3 Tambau mutant is retained in a pre-medial Golgi compartment likely due misorientation. 

Figure 16 Effects of pH and salt type on band spacing in the anion-exchange separation of a protein sample 1, myoglobin 2, transferrin 3, a,-acid glycoprotein 4, a-lactalbumin 5, soybean trypsin inhibitor. Conditions 5 x 0.4-cm WAX column (300A pore) (Shimadzee Shim-pack) 0-100% B in 20min I.OmL/min. (a) A solvent, 0.02 M phosphate buffer B solvent, 0.5 M phosphate buffer (b) A solvent, 0.02 M phosphate buffer B solvent 0.5 M NaCI or Na2S04. (From Ref. 41.)...

Liu DS, Kennedy SD and Knauf PA (1996) Source of transport site asymmetry in the band-3 anion exchange protein determined by NMR measurements of external Cr affinity. Biochemistry 35 15228-15235. 

---