Band 4.1 protein

Jennings, M.L., and Nicknish, J.S. (1985) Localization of a site of intermolecular cross-linking in human red blood cell band 3 protein./. Biol. Chem. 260, 5472-5479. 

Several derivatives of Eosin have been prepared and employed to study biological systems. Their main applications are as singlet energy acceptors and as triplet probes [93-97] to measure the rotational mobility of virus particles [98] and proteins in membranes and in solution. Examples of proteins studied using Eosin derivatives include myosin [99,100], band 3 protein [101,102], pyruvate dehydrogenase [103,104], and Sarcoplasmic... 

The localization of the sensitizer has a significant effect on the photodynamic activity. Eosin is scarcely taken up by cells, and Pooler and Girotti [131] report that Eosin isothiocyanate is 50-100 times more efficient for inducing photohemolysis of human erythrocytes. The spectral properties and quantum yields for singlet oxygen production are identical for both compounds. Therefore, they attribute the difference in photodynamic activity to the ability of the isothiocyanate derivative to bind covalently to band 3 protein. 

Related proteins occur in other tissues.488 The 911-residue band 3 protein consists of two distinct parts of nearly equal size. The N-terminal portion is attached to the membrane skeleton (Fig. 8-16). The C-terminal part, which is embedded in the membrane, is thought to form 14 transmembrane helices and to contain the ion exchange channel or channels.4893 As previously mentioned, defects in the N-terminal portion cause spherocytosis. The mutation Arg 589 His in the C-terminal half causes renal tubular acidosis in which the kidneys do not adequately remove acids from the body.238 489 Band 3 proteins can also exchange phosphate, sulfate, and phosphoenolpyruvate for Cl or bicarbonate. 

Erythrocyte membranes band 3 protein 420 proteins of 403 Erythrose 163s Erythrulose 164s Escherichia coli 3... 

One of the major integral proteins of the erythrocyte membrane is the anion channel, or band-3 protein, which moves Cl- and HC03 anions across the membrane. The anion transporter has two identical subunits with molecular weights of about 95,000, and each subunit probably has 10 or 11 transmembrane helices. The band-3 protein is attached to the spectrin cytoskeleton through a smaller protein, anky-rin. The cytosolic domain of the anion transporter also binds the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. 

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