Results 271 to 280 of about 87,526 (316)
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Interaction of ticlopidine with the erythrocyte membrane
Biochemical Pharmacology, 1982The membrane effects of ticlopidine on the erythrocyte membrane were explored by the spin label method at the proteic and phospholipidic levels. This spectroscopic study was completed by polyacrylamide gel electrophoresis of proteins, measurement of the protection against haemolysis and observation of the erythrocyte shape changes induced by the drug ...
Magali Sablayrolles +3 more
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Proteins of the camel erythrocyte membrane
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1975Electrophoresis on polyacrylamide gels containing dodecyl sulphate has revealed that the major proteins of the camel erythrocyte membrane are similar to those of the human and bovine species in both electrophoretic mobility and relative abundance. The major difference lies in the major intrinsic membrane protein of molecular weight approx. 100 000.
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Surface proteins of erythrocyte membranes
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1971Abstract Diazotized sulfanilic acid labeling and trypsin digestion studies of human and bovine erythrocytes indicate that the glycoprotein of each species is the only major membrane protein which is readily accessible at the cell surface. Trypsin digestion of isolated human erythrocyte membranes under conditions identical to the erythrocyte digestion
Kermit L. Carraway +2 more
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Calcium binding by the erythrocyte membrane
Biochimica et Biophysica Acta (BBA) - Biomembranes, 1973Abstract Calcium binding to isolated erythrocyte membranes was stimulated by ATP. This stimulatory effect of ATP required Mg 2+ . Ethacrynic acid and ruthenium red inhibited the stimulatory effect of ATP. About 80% of the bound Ca 2+ was associated with the membrane protein.
V. Schwarz, Michael J. Duffy
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Proteins of the turkey erythrocyte membrane
Biochemistry, 1976A new and simplified method is described for preparation of turkey erythrocyte membranes which are essentially devoid of supernatant or nuclear contamination, but retain catecholamine-sensitive adenylate cyclase activity. These membranes have been solubilized in sodium dodecyl sulfate and analyzed by polyacrylamide gel electrophoresis and the major ...
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Sphingomyelinase of chicken erythrocyte membranes
Archives of Biochemistry and Biophysics, 1975Abstract Most of the chicken erythrocyte's sphingomyelin is hydrolyzed when the chicken red blood cells are incubated in hypotonie solution at 37 °C. Addition of detergents, such as Triton X-100 or Na-cholate, is essential for hydrolysis of external [3H ]sphingomyelin by the erythrocyte membranes.
Abraham Loyter, Daniella Hirshfeld
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Adsorptive immobilization of erythrocyte membrane
Journal of Biotechnology, 2000Immobilization of human erythrocyte membrane was carried out by adsorption on Fractosil, a porous form of silica. Acetylcholinesterase (AChE) was chosen as a representative membrane enzyme in this study. Dependency of adsorption on membrane concentration was determined.
Sadighe Khezre-Barati +3 more
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Carcinoembryonic Antigens of Erythrocyte Membranes
Nature New Biology, 1973The carcinoembryonic antigen (CEA) of Gold and Freed-man1 was first described as being specific for tumours and foetal tissue of endodermal origin. This glycoprotein, or some antigenically related counterpart, has been shown by radioimmunoassay and other procedures to occur in the urine, plasma and faeces of healthy subjects and in patients bearing a ...
A. L. Barsoum +3 more
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Erythrocyte Membrane: Chemical Modification
Science, 1965Erythrocytes treated with 1-fluoro-2,4-dinitrobenzene become permeable to Na + and K + , but not to small water-soluble nonelectrolytes or hemoglobin, and eventually lyse in isotonic buffer. Erythrocytes treated with 1,5-difluoro-2,4-dinitrobenzene become permeable to Na +
Howard C. Berg +2 more
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The Erythrocyte Membrane Skeleton: Pathophysiology
Hospital Practice, 1984Given the evident importance of the membrane skeleton in preserving shape and structural integrity of the erythrocyte, one would expect that disorders involving abnormalities of shape or fragility ...
Samuel E. Lux, Stephen B. Shohet
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