scholarly journals Localization of the protein 4.1-binding site on human erythrocyte glycophorins C and D

1994 ◽  
Vol 300 (3) ◽  
pp. 920-920 ◽  
Keyword(s):  
Binding Site ◽  
Human Erythrocyte ◽  
Protein 4.1

scholarly journals Mapping the ankyrin-binding site of the human erythrocyte anion exchanger

1989 ◽  
Vol 264 (16) ◽  
pp. 9665-9672 ◽  
Author(s):  
L Davis ◽  
S E Lux ◽  
V Bennett
Keyword(s):  
Binding Site ◽  
Anion Exchanger ◽  
Human Erythrocyte

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 The human erythrocyte anion transport protein, band 3. Characterization of exofacial alkaline titratable groups involved in anion binding/translocation.

1992 ◽  
Vol 100 (2) ◽  
pp. 301-339 ◽  
Author(s):  
P J Bjerrum
Keyword(s):  
Ionic Strength ◽  
Binding Site ◽  
Transport System ◽  
Human Erythrocyte ◽  
Binding Constant ◽  
Anion Transport ◽  
High Ionic Strength ◽  
Anion Binding ◽  
Asymmetry Factor ◽  
Sensitive Group

Chloride self-exchange across the human erythrocyte membrane at alkaline extracellular pH (pHO) and constant neutral intracellular pH (pH(i)) can be described by an exofacial deprotonatable reciprocating anion binding site model. The conversion of the transport system from the neutral to the alkaline state is related to deprotonation of a positively charged ionic strength- and substrate-sensitive group. In the absence of substrate ions ([ClO] = 0) the group has a pK of approximately 9.4 at constant high ionic strength (equivalent to approximately 150 mM KCl) and a pK of approximately 8.7 at approximately zero ionic strength. The alkaline ping-pong system (examined at constant high ionic strength) demonstrates outward recruitment of the binding sites with an asymmetry factor of approximately 0.2, as compared with the inward recruitment of the transport system at neutral pHO with an asymmetry factor of approximately 10. The intrinsic half-saturation constant for chloride binding, with [Cli] = [Clo], increased from approximately 30 mM at neutral to approximately 110 mM at alkaline pHO. The maximal transport rate was a factor of approximately 1.7 higher at alkaline pHO. This increase explains the stimulation of anion transport, the "modifier hump," observed at alkaline pHO. The translocation of anions at alkaline pHO was inhibited by deprotonation of another substrate-sensitive group with an intrinsic pK of approximately 11.3. This group together with the group with a pK of approximately 9.4 appear to form the essential part of the exofacial anion binding site. The effect of extracellular iodide inhibition on chloride transport as a function of pHO could, moreover, be simulated if three extracellular iodide binding constants were included in the model: namely, a competitive intrinsic iodide binding constant of approximately 1 mM in the neutral state, a self-inhibitor binding constant of approximately 120 mM in the neutral state, and a competitive intrinsic binding constant of approximately 38 mM in the alkaline state.

Mapping the tropomyosin isoform 5 binding site on human erythrocyte tropomodulin: Further insights into E-Tmod/TM5 interaction

2005 ◽  
Vol 444 (2) ◽  
pp. 130-138 ◽  
Author(s):  
Carlos Vera ◽  
Jianmin Lao ◽  
Donald Hamelberg ◽  
Lanping Amy Sung
Keyword(s):  
Binding Site ◽  
Human Erythrocyte

Synthesis and Characterization of a Novel Spin-Labeled Affinity Probe of Human Erythrocyte Band 3:  Characteristics of the Stilbenedisulfonate Binding Site†

Biochemistry ◽  
1996 ◽  
Vol 35 (21) ◽  
pp. 6931-6943 ◽  
Author(s):  
Douglas J. Scothorn ◽  
Walter E. Wojcicki ◽  
Eric J. Hustedt ◽  
Albert H. Beth ◽  
Charles E. Cobb
Keyword(s):  
Binding Site ◽  
Human Erythrocyte ◽  
Band 3 ◽  
Synthesis And Characterization ◽  
Affinity Probe

scholarly journals Erythrocyte adducin: a calmodulin-regulated actin-bundling protein that stimulates spectrin-actin binding.

1987 ◽  
Vol 105 (6) ◽  
pp. 2837-2845 ◽  
Author(s):  
S M Mische ◽  
M S Mooseker ◽  
J S Morrow
Keyword(s):  
Ionic Strength ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Actin Binding ◽  
Protein 4.1 ◽  
Calcium Dependent ◽  
High Affinity ◽  
Putative Role ◽  
Cross Bridges ◽  
Dependent Mechanism

Adducin is an erythrocyte membrane skeletal phosphoprotein comprised of two related subunits of 105,000 and 100,000 Mr. These peptides form a functional heterodimer, and the smaller of the two binds calmodulin in a calcium-dependent fashion. Although this protein has been physicochemically characterized, its function remains unknown. We have examined the interaction of human adducin with actin and with human erythrocyte spectrin using sedimentation, electrophoretic, and morphologic techniques. Purified adducin binds actin at physiologic ionic strength and bundles it into arrays of laterally arranged filaments, the adducin forming cross-bridges between the filaments at 35.2 /- 3.8 (2 SD) nm intervals. The stoichiometry of high affinity adducin binding to actin at saturation is 1:7, corresponding to a dimer of adducin for every actin helical unit. Adducin also promotes the binding of spectrin to actin independently of protein 4.1. At saturation, each adducin promotes the association of one spectrin heterodimer. The formation of this ternary spectrin-actin-adducin complex is independent of the assembly path, and the complex exists in a readily reversible equilibrium with the free components. The binding of adducin to actin and its ability to stimulate spectrin-actin binding is down-regulated by calmodulin in a calcium-dependent fashion. These results thus identify a putative role for adducin, and define a calcium- and calmodulin-dependent mechanism whereby higher states of actin association and its interaction with spectrin in the erythrocyte may be controlled.

scholarly journals Purification of the NF2 Tumor Suppressor Protein from Human Erythrocytes

2006 ◽  
Vol 33 (4) ◽  
pp. 394-402 ◽  
Author(s):  
Hitesh K. Jindal ◽  
Kazumi Yoshinaga ◽  
Pil-Soo Seo ◽  
Mohini Lutchman ◽  
Patrick A. Dion ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Tumor Suppressor ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Mammalian Cells ◽  
Tumor Suppressor Protein ◽  
Human Erythrocyte Membrane ◽  
Protein 4.1 ◽  
Erythrocyte Plasma Membrane ◽  
Inside Out

Background:Neurofibromatosis type 2 (NF2) is an autosomal dominant disease predisposing individuals to the risk of developing tumors of cranial and spinal nerves. The NF2 tumor suppressor protein, known as Merlin/Schwanomin, is a member of the protein 4.1 superfamily that function as links between the cytoskeleton and the plasma membrane.Methods:Upon selective extraction of membrane-associated proteins from erythrocyte plasma membrane (ghosts) using low ionic strength solution, the bulk of NF2 protein remains associated with the spectrin-actin depleted inside-out-vesicles. Western blot analysis showed a ~70 kDa polypeptide in the erythrocyte plasma membrane. Furthermore, quantitative removal of NF2 protein from the inside-out-vesicles was achieved using 1.0 M potassium iodide, a treatment known to remove tightly-bound peripheral membrane proteins.Results:These results suggest a novel mode of NF2 protein association with the erythrocyte membrane that is distinct from the known membrane interactions of protein 4.1. Based on these biochemical properties, several purification strategies were devised to isolate native NF2 protein from human erythrocyte ghosts. Using purified and recombinant NF2 protein as internal standards, we quantified approximately ~41-65,000 molecules of NF2 protein per erythrocyte.Conclusion:We provide evidence for the presence of NF2 protein in the human erythrocyte membrane. The identification of NF2 protein in the human erythrocyte membrane will make it feasible to discover novel interactions of NF2 protein utilizing powerful techniques of erythrocyte biochemistry and genetics in mammalian cells.

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