Comparative aspects of phosphate transfer across mammalian erythrocyte membranes

1973 ◽  
Vol 13 (1) ◽  
pp. 19-36 ◽  
Author(s):  
W. Gruber ◽  
B. Deuticke
Keyword(s):  
Erythrocyte Membranes ◽  
Mammalian Erythrocyte

A Comparative Protein Profile of Mammalian Erythrocyte Membranes Identified by Mass Spectrometry

2014 ◽  
Vol 247 (11) ◽  
pp. 1181-1189 ◽  
Author(s):  
Savita Sharma ◽  
Vinny Punjabi ◽  
Surekha M. Zingde ◽  
Sadashiv M. Gokhale
Keyword(s):  
Mass Spectrometry ◽  
Protein Profile ◽  
Erythrocyte Membranes ◽  
Mammalian Erythrocyte

scholarly journals Impact of membranetropic compounds on the sensitivity of mammalian erythrocytes to the posthypertonic shock action

2020 ◽  
pp. 31-38
Author(s):  
O Chabanenko ◽  
◽  
N Yershova ◽  
N Orlova ◽  
N Shpakova ◽  
...  
Keyword(s):  
Critical Micelle Concentration ◽  
Defect Formation ◽  
Phospholipid Composition ◽  
Erythrocyte Membranes ◽  
Minimum Level ◽  
Rat Erythrocytes ◽  
Amphiphilic Compounds ◽  
Antihemolytic Activity ◽  
Mammalian Erythrocyte ◽  
Shock Action

The effect of cationic trifluoperazine (TFP) and nonionic decyl-β,D-glucopyranoside (DGP) on the sensitivity of human, rabbit and rat erythrocytes to the action of posthypertonic shock (PHS) at 0 °C was studied in this research. Trifluoperazine shows a high antihemolytic activity under conditions of PHS of human and animal erythrocytes at slight differences of values of effective concentrations. The value of antihemolytic activity of TFP for human and rabbit erythrocytes is ~ 60 %, and for rat cells the efficiency of this compound is approximately 1.4 times higher. The values of antihemolytic activity of DGP under PHS conditions of human and rat erythrocytes are comparable and amounts to 62 and 66 %, respectively. Significant differen­ces of this parameter (72 %) were found for rabbit cells compared with human erythrocytes. It was found that the size of plateau (the range of concentrations of amphiphilic compounds within the minimum level of erythrocyte hemolysis was observed) cationic TFP and nonionic DGP are significantly different. Thus, TFP has a narrow plateau (100–200 μmol/L), while DGP has a rather wide one (400–1600 μmol/L). In addition, a shift of the plateau concentrations of DGP to the region of higher values compared with TFP is observed, which is probably due to the fact that the value of the critical micelle concentration DGP is higher than TFP. Moreover, a shift of plateau concentrations of DGP to the region of higher values compared with TFP is observed, that is probably due to the fact that the value of the critical micelle concentration DGP is higher than TFP one. It was established that under PHS conditions of human erythrocyte, both compounds (TFP and DGP) show a commensurate antihemolytic activity. At the same time, for rabbit cells, DGP is more effective compared with TFP, and for rat erythrocytes, on the contrary, the efficiency of TFP is higher than DGP. This may be due to differences in the phospholipid composition of mammalian erythrocyte membranes. The results suggest that under PHS conditions the efficacy of membrane-tropic compounds is most likely due to their ability to incorporate into membrane to the defect formation areas, and thus significantly increase the critical hemolytic volume of cells, as a result, prevent their destruction.

scholarly journals Calcium and Magnesium Contents of Mammalian Erythrocyte Membranes

1973 ◽  
Vol 21 (1) ◽  
pp. 171-175 ◽  
Author(s):  
TATSUZO FUJII ◽  
TAKASHI SATO ◽  
TAKASHI HANZAWA
Keyword(s):  
Erythrocyte Membranes ◽  
Mammalian Erythrocyte ◽  
Calcium And Magnesium

Effect of Integral Proteins on Frozen Membrane Fracture

1980 ◽  
Vol 38 ◽  
pp. 756-759 ◽  
Author(s):  
S. Kirchanski ◽  
D. Branton
Keyword(s):  
Lipid Bilayers ◽  
Freeze Fracture ◽  
Covalent Bond ◽  
Erythrocyte Membranes ◽  
Glycophorin A ◽  
Experimental Protocol ◽  
Transmembrane Glycoprotein ◽  
Bond Breakage ◽  
Human Erythrocyte Membranes ◽  
Integral Proteins

We have investigated the effect of integral membrane proteins upon the fracturing of frozen lipid bilayers. This investigation has been part of an effort to develop freeze fracture labeling techniques and to assess the possible breakage of covalent protein bonds during the freeze fracture process. We have developed an experimental protocol utilizing lectin affinity columns which should detect small amounts of covalent bond breakage during the fracture of liposomes containing purified (1) glycophorin (a transmembrane glycoprotein of human erythrocyte membranes). To fracture liposomes in bulk, frozen liposomes are ground repeatedly under liquid nitrogen. Failure to detect any significant covalent bond breakage (contrary to (2)) led us to question the effectiveness of our grinding procedure in fracturing and splitting lipid bilayers.

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