Effect of membrane potential on band 3 conformation in the human erythrocyte membrane detected by triplet state quenching experiments

Biochemistry ◽  
1992 ◽  
Vol 31 (19) ◽  
pp. 4650-4656 ◽  
Author(s):  
Katrina Wyatt ◽  
Richard J. Cherry
Keyword(s):  
Membrane Potential ◽  
Triplet State ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Human Erythrocyte Membrane

scholarly journals The aldolase-binding site of the human erythrocyte membrane is at the NH2 terminus of band 3.

1981 ◽  
Vol 256 (21) ◽  
pp. 11203-11208 ◽  
Author(s):  
S.N. Murthy ◽  
T. Liu ◽  
R.K. Kaul ◽  
H. Köhler ◽  
T.L. Steck
Keyword(s):  
Binding Site ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Human Erythrocyte Membrane

scholarly journals Phosphotyrosine phosphatase associated with band 3 protein in the human erythrocyte membrane

1996 ◽  
Vol 314 (3) ◽  
pp. 881-887 ◽  
Author(s):  
Yehudit ZIPSER ◽  
Nechama S. KOSOWER
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Intact Cell ◽  
Band 3 ◽  
Band 3 Protein ◽  
Human Erythrocyte Membrane ◽  
Major Fraction ◽  
Phosphotyrosine Phosphatase ◽  
A Minor ◽  
Triton X

The anion-exchange band 3 protein is the main erythrocyte protein that is phosphorylated by tyrosine kinase. To study the regulation of band 3 phosphorylation, we examined phosphotyrosine phosphatase (PTP) activity in the human erythrocyte. We show that the human erythrocyte membrane contains a band 3-associated neutral PTP which is activated by Mg2+ and inhibited by Mn2+ and vanadate. The PTP is active in the intact cell and in the isolated membrane. A major fraction of the PTP is tightly bound to the membrane and can be extracted from it by Triton X-100; a minor part is associated with the Triton X-100-insoluble cytoskeleton. The behaviour of the PTP parallels that of band 3, the major fraction of which is extractable by detergents with a minor fraction being anchored to the cytoskeleton. Moreover, band 3 is co-precipitated when the PTP is immunoprecipitated from solubilized membranes, and PTP is co-precipitated when band 3 is immunoprecipitated. The PTP appears to be related to PTP1B (identified using an antibody to an epitope in its catalytic domain and by molecular mass). The system described here has a unique advantage for PTP research, since it allows the study of the interaction of a PTP with an endogenous physiological substrate that is present in substantial amounts in the cell membrane. The membrane-bound, band 3-associated, PTP may play a role in band 3 function in the erythrocyte and in other cells which have proteins analogous to band 3.

scholarly journals Cytoskeleton-membrane connections in the human erythrocyte membrane: band 4.1 binds to tetrameric band 3 protein

1997 ◽  
Vol 1325 (2) ◽  
pp. 226-234 ◽  
Author(s):  
Bogdan von Rückmann ◽  
Thomas Jöns ◽  
Frank Dölle ◽  
Detlev Drenckhahn ◽  
Dieter Schubert
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Band 3 Protein ◽  
Human Erythrocyte Membrane

scholarly journals Identification of Contact Sites between Ankyrin and Band 3 in the Human Erythrocyte Membrane

Biochemistry ◽  
2012 ◽  
Vol 51 (34) ◽  
pp. 6838-6846 ◽  
Author(s):  
Jesse L. Grey ◽  
Gayani C. Kodippili ◽  
Katya Simon ◽  
Philip S. Low
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Human Erythrocyte Membrane ◽  
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