Rabbit erythrocyte membranes

Fig. 11.—Sequence of a 2S-Sugar Residue Glycosphingolipid Isolated from Rabbit Erythrocyte Membranes. (Cleavage points, and the masses of fragment ions of the permethylated derivative, are shown. No fragment-ions were observed above 4000, because of the poor sensitivity at high mass.)...

Inhibited HgCl2-induced rabbit erythrocyte membrane damage 380... 

Matsuzaki, Y, Ito, Y, Nakahara, Y, Ogawa, T, Synthesis of branched poly-A-acetyl-lactosamine type pentaantennary pentacosasaccharide glycan part of a glycosyl ceramide from rabbit erythrocyte membrane. Tetrahedron Lett., 34, 1061-1064, 1993. 

Anthocyanin pigments, such as cyanidin 3-glucoside and its aglycone cyanidin, showed antioxidant activity in four different lipid oxidation sytems the linoleic acid autoxidation system, the egg lecithin liposomes system, the rabbit erythrocyte membrane system and the rat liver microsomal system [94]. Anthocyanins from eggplant [127], grape [91] and red beans [128], also show significant antioxidant activity. 

Erythrocytes do not contain mitochondria and any anion-sensitive ATPase activity in a particulate fraction must therefore be attributed to the plasma membrane. An Mg-ATPase, which could be stimulated by bicarbonate was found in rabbit erythrocyte membranes [31-33] and should thus be plasma-membrane bound. The properties of the enzyme in rabbit erythrocyte membranes are, however, completely different from those of the anion-sensitive ATPase from other tissues. Whereas sulfite is a good stimulant for the Mg-ATPase in mitochondrial and microsomal fractions of various tissues, it only slightly stimulates [32] or even inhibits [33] the erythrocyte enzyme. Other oxy-anions inhibit the ATPase of erythrocyte membranes [32]. The substrate dependence of the enzyme is greatly different from that of the enzyme from other tissues [32,33]. The half maximal inhibitory concentration of... 

Applications of fast atom bombardment (FAB)-m.s. and laser desorption-m.s. in the analysis of complex human milk oligosaccharides, phosphoinositol-linked glycans from surface glycoproteins, and high molecular weight glycosphingolipids (with up to 40 sugar residues) present in rabbit erythrocyte membranes, have been reviewed (45 refs.). ... 

Kato, I., and Naiki, M., 1976, Ganglioside and rabbit erythrocyte membrane receptor for Staphylococcal alpha-toxin. Infect. Immun. 13 289-291. 

In the absence of activators AMP aminohydrolase from brain (149), erythrocytes (143, 150), muscle (145), and liver (128) gave sigmoid curves for velocity vs. AMP concentration which were hyperbolic after the addition of monovalent cations, adenine nucleotides, or a combination of monovalent cations and adenine nucleotides. For the rabbit muscle enzyme (145), addition of K+, ADP, or ATP produced normal hyperbolic saturation curves for AMP as represented by a change in the Hill slope nH from 2.2 to 1.1 Fmax remained the same. The soluble erythrocyte enzyme and the calf brain enzyme required the presence of both monovalent cations and ATP before saturation curves became hyperbolic. In contrast, the bound human erythrocyte membrane enzyme did not exhibit sigmoid saturation curves and K+ activation was not affected by ATP (142). 

In 1979, Jette E. Kristiansen of Copenhagen, Denmark, performed extensive experiments to elaborate the effect of chlorpromazine on the permeability of the bacterial cell wall [55]. In vitro experiments were carried out with Staphylococcus aureus under the influence of chlorpromazine. Depigmentation and bacteriostatic/bactericidal effects of chlorpromazine on the microorganisms were observed. It has been shown that concentrations of chlorpromazine near the bacteriostatic value, in combination with bacterial haemolysins, could alter erythrocyte membranes of horse and rabbit blood in such a way that they become resistant to haemolysis. It was further realized that chlorpromazine in bacteriostatic concentration probably changed the transport of potassium through the bacterial membrane in the same manner as described for mammalian muscle tissue [54],... 

Rabbit erythrocytes exposed to low concentrations of puromycin (7 x 10 " moll ) caused disruption of cell membrane indicating inhibition of protein synthesis by erythrocytes. Puromycin is shown to cause nephrosis in rats. It is a glomerular nephrotoxi-cant and is extensively used to study pathophysiology of glomerular nephritis and nephrotic syndrome. 

Figure 2. Inhibitory potency of suramin and of three of its analogues (for chemical structure, see Figure 1) at P2X P2Y"Purinoceptors. — Inhibition of neurogenic contractions (0.05 Hz plCfo values) in rabbit vas deferens (P2X-receptors). -- Inhibition of ADP(3 binding (pKj values) to turkey erythrocyte membranes (P2Y- "sceptors) [35].

Hemolysis data are known to provide a simple and reliable measure for the estimation of CyD-induced membrane damage or cytotoxicity [10, 14). Figure 14.2 shows the hemolysis curves of hydrophilic CyDs on rabbit erythrocytes. The hemolytic effects of methylated CyDs are much higher than those of other CyDs [32, 33). In a series of CyD derivatives, there is a positive correlation between the hemolytic activity and their capacity to solubilize the lipophilic components of the cell membranes (cholesterol and phospholipids). Since the methylated CyDs remove cholesterol significantly from human intestinal epithelial cell monolayers [34], this will... 

A fluorimetric method for the thermodynamic and kinetic interpretation of lectin-receptor reactions has been validated in a study of the binding of rabbit erythrocytes to Lens culinaris lectin conjugated with fluorescein. It was demonstrated that under conditions when even a low number of receptors are saturated, most lectin molecules are univalently bound to the receptor. The high affinity for the membrane receptor, contrasting with the low affinity for specific monosaccharides, is explained by the very slow dissociation reaction which requires twice the energy of the association reaction. 

The amoeba Acanthamoeba castellani has been shown to bind to equine erythrocytes by interaction with carbohydrates on the surface of the red cells. 4-Nitrophenyl tri-A-methyltyrosinate [ I]iodide has been used to label the outer surface of mature chicken erythrocytes. Two component glycoproteins, with subunits of molecular weight 5 x 10 and 1 x 10 , were identified. Neuraminidase-treated rat and rabbit erythrocytes were shown to be rapidly sequestered by the liver. Chemical studies of glycoproteins obtained from erythrocyte membranes from a number of sources have been reported. ... 

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