Results 361 to 370 of about 2,250,672 (421)
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Calcium binding to the erythrocyte membrane
Acta Histochemica, 1976Calcium binding sites of human red blood cells were localized by means of a method according to OSCHMAN and WALL (1972). The procedure resulted in multiple opaque deposits at the inner surface of the erythrocyte membrane.
Günther Geyer, Werner Linss
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Membrane transport in the malaria parasite and its host erythrocyte.
Biochemical Journal, 2014As it grows and replicates within the erythrocytes of its host the malaria parasite takes up nutrients from the extracellular medium, exports metabolites and maintains a tight control over its internal ionic composition.
K. Kirk, Adele M. Lehane
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Erythrocyte Membrane Elasticity and Viscosity
Annual Review of Physiology, 1987The classical theory of elasticity (35) treats the material of a deformable body as a three-dimensional continuum in which internal stresses occur as the body is deformed by external forces acting over its surface. Although the internal stresses are caused by the displacement of atoms or molecules from an original state of equilibrium, the molecular ...
Richard E. Waugh, Robert M. Hochmuth
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The phosphoproteins of the sickle erythrocyte membrane
Archives of Biochemistry and Biophysics, 1986The uptake of 32P from exogenous 32Pi into membrane proteins of sickle erythrocytes has been analyzed. The phosphorylation of spectrin is normal in sickle cells. There is, however, a substantial increase in 32P in the sialoproteins of the membrane, which can be demonstrated after fractionation or selective proteolysis.
James K. Dzandu +2 more
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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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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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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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1995
The majority of the blood group characters treated in this monograph are defined as serological properties of the erythrocyte membrane. The expression of these characters is highly influenced by the structure and prevailing constitution of the membrane. It is therefore appropriate to present a concise survey on membrane composition and structure.
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The majority of the blood group characters treated in this monograph are defined as serological properties of the erythrocyte membrane. The expression of these characters is highly influenced by the structure and prevailing constitution of the membrane. It is therefore appropriate to present a concise survey on membrane composition and structure.
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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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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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