Changes in Human Erythrocyte Membrane Proteins During Storage

Vox Sanguinis ◽  
1971 ◽  
Vol 20 (3) ◽  
pp. 239-251
Author(s):  
G.L. Moore ◽  
D.A. Cooper ◽  
R.S. Antonoff ◽  
S.L. Robinson
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Proteins

Reaction of acetaldehyde with human erythrocyte membrane proteins

FEBS Letters ◽  
1977 ◽  
Vol 75 (1-2) ◽  
pp. 115-119 ◽  
Author(s):  
Katherine C. Gaines ◽  
J.M. Salhany ◽  
D.J. Tuma ◽  
M.F. Sorrell
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Proteins

scholarly journals Erythrocyte membrane inhibitor of reactive lysis: effects of phosphatidylinositol-specific phospholipase C on the isolated and cell- associated protein

Blood ◽  
1990 ◽  
Vol 75 (1) ◽  
pp. 284-289 ◽  
Author(s):  
MH Holguin ◽  
LA Wilcox ◽  
NJ Bernshaw ◽  
WF Rosse ◽  
CJ Parker
Keyword(s):  
Membrane Proteins ◽  
Phospholipase C ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Paroxysmal Nocturnal Hemoglobinuria ◽  
Membrane Attack Complex ◽  
Human Erythrocyte Membrane ◽  
Glycosyl Phosphatidylinositol ◽  
Normal Human ◽  
Erythrocyte Membrane Proteins

Abstract The erythrocyte membrane inhibitor of reactive lysis (MIRL) is an 18-Kd protein that controls complement-mediated hemolysis by restricting the activity of the membrane attack complex. MIRL expression on the erythrocytes of paroxysmal nocturnal hemoglobinuria (PNH) is abnormally low, and the greater susceptibility of PNH erythrocytes to complement is causally related to this deficiency. Inasmuch as other proteins that are deficient in PNH are anchored to the membrane through a glycosyl phosphatidylinositol moiety, studies were undertaken to determine if MIRL shares this structural feature. Normal human erythrocytes that had been radiolabeled with 125I were incubated with phosphatidylinositol- specific phospholipase C (PIPLC), and the supernate and the solubilized membrane proteins were immunoprecipitated using anti-MIRL antiserum. The MIRL that was specifically released into the supernate had an Mr of 19 Kd, while the MIRL that remained bound to the membrane had an Mr of 18 Kd. A quantitative assay showed that approximately 10% of erythrocyte MIRL was susceptible to PIPLC; however, treatment with PIPLC had no effect on either the electrophoretic mobility or the functional activity of purified MIRL. These studies show that the effects of PIPLC on MIRL are similar to those observed for other human erythrocyte membrane proteins that are anchored by a glycosyl phosphatidylinositol moiety.

Interaction of molybdenum with human erythrocyte membrane proteins

1980 ◽  
Vol 2 (1) ◽  
pp. 57-64 ◽  
Author(s):  
Marie Kselíková ◽  
Tomáš Mařík ◽  
Bedřich Bíbr ◽  
Jaroslav Lener
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Proteins

Changes in Human Erythrocyte Membrane Proteins During Storage

Vox Sanguinis ◽  
1971 ◽  
Vol 20 (3) ◽  
pp. 239-251 ◽  
Author(s):  
G. L. Moore ◽  
D. A. Cooper ◽  
R. S. Antonoff ◽  
S. L. Robinson
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Proteins

scholarly journals An Improved 2-Dimensional Gel Electrophoresis Method for Resolving Human Erythrocyte Membrane Proteins

2017 ◽  
Vol 8 ◽  
pp. 117864181770088 ◽  
Author(s):  
Manoj Kumar ◽  
Rajendra Singh ◽  
Anil Meena ◽  
Bhagwan S Patidar ◽  
Rajendra Prasad ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Isoelectric Focusing ◽  
Human Erythrocyte ◽  
Gel Electrophoresis ◽  
Protein Extraction ◽  
Therapeutic Potential ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Proteins

The 2-dimensional gel electrophoresis (2-DE) technique is widely used for the analysis of complex protein mixtures extracted from biological samples. It is one of the most commonly used analytical techniques in proteomics to study qualitative and quantitative protein changes between different states of a cell or an organism (eg, healthy and diseased), conditionally expressed proteins, posttranslational modifications, and so on. The 2-DE technique is used for its unparalleled ability to separate thousands of proteins simultaneously. The resolution of the proteins by 2-DE largely depends on the quality of sample prepared during protein extraction which increases results in terms of reproducibility and minimizes protein modifications that may result in artifactual spots on 2-DE gels. The buffer used for the extraction and solubilization of proteins influences the quality and reproducibility of the resolution of proteins on 2-DE gel. The purification by cleanup kit is another powerful process to prevent horizontal streaking which occurs during isoelectric focusing due to the presence of contaminants such as salts, lipids, nucleic acids, and detergents. Erythrocyte membrane proteins serve as prototypes for multifunctional proteins in various erythroid and nonerythroid cells. In this study, we therefore optimized the selected major conditions of 2-DE for resolving various proteins of human erythrocyte membrane. The modification included the optimization of conditions for sample preparation, cleanup of protein sample, isoelectric focusing, equilibration, and storage of immobilized pH gradient strips, which were further carefully examined to achieve optimum conditions for improving the quality of protein spots on 2-DE gels. The present improved 2-DE analysis method enabled better detection of protein spots with higher quality and reproducibility. Therefore, the conditions established in this study may be used for the 2-DE analysis of erythrocyte membrane proteins for different diseases, which may help to identify the proteins that may serve as markers for diagnostics as well as targets for development of new therapeutic potential.

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