Erythrocyte from rabbit

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.)...

Figure 4. Comparison of the uptake of Li+ into erythrocytes from rat and rabbit, determined by 7Li NMR spectroscopy [34],...

Parallel activation of Na+/H+ antiport and CI7HCO3 antiport Erythrocytes from dog, rabbit, and Amphiuma lymphocytes osteoclasts endothelial cells parotis pancreas, liver, gallbladder, proximale tubule, medullary thick ascending limb, and collecting duct MDCK cells Activation of Na+-K+-2CI cotransport... 

Erythrocytes from humans, birds, and rat Ehrlich ascites tumor cells astrocytes fibroblasts C67 glioma cells intestine trachea parotid MDCK cells retinal pigment epithelium frog skin HeLa cells rabbit medullary thick ascending limb Inhibition of K+ and Cl channels... 

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. 

The role of erythrocytes in vitamin B6 metabolism remains uncertain. Mouse and human erythrot es have higher oxidase activity and, therefore, convert pyridoxine to pyridoxal phosphate appreciably faster than erythrocytes from rat, hamster, and rabbit (Fonda, 1988). Anemic rats showed increased urinary loss of label administered as pyridoxal, suggesting that uptake by erythrocytes may conserve pyridoxal (Ink and Henderson, 1984). 

A unique lipoxygenase was isolated and purified from rabbit reticulocytes [212], The purified enzyme with a molecular weight of 78000 contains two moles of iron per enzyme molecule. The enzyme is identical with the previously known protein factors which inhibit the respiratory chain. The purified lipoxygenase causes a loss of acid-labile sulfur from mitochondrial electron transfer particles and acts preferably on the mitochondrial membrane. The enzyme is considered to work in the lysis of mitochondria during the maturation of erythrocytes. The major product from arachidonic acid is 15S-hydroperoxy-5,8,l 1,13-eicosatetraenoic acid, although the 12S-hydroperoxy derivative is produced as a minor product [213]. 

Lipoxygenase has been extensively studied with a purified preparation from rabbit reticulocytes [40,48]. In the course of reticulocyte maturation, the decline in 15-lipoxygenase appeared concomitantly with the breakdown of mitochondria, and mature erythrocytes have no 15-lipoxygenase [40]. In human tissues, eosinophils [134,135] and airway epithelial cells [78,136] are major sources... 

Plasma membranes from rabbit reticulocytes, but not those from erythrocytes, are able to glycosylate endogenous proteins through dolichyl-bound sugar derivatives. ... 

When rabbits are injected with other animal tissue, the Forssman haptens are produced. These are able to lyse erythrocytes from sheep (Forssman 1911). One of these Forssman haptens is a ceramide linked to galactose and galactosamine (Papirmeister et al. 1955). The structure of these haptens leaves the question open whether they arise from ceramide polyhexosides, e.g. globosides, by degradation. It should be mentioned that the only noncarbohydrate lipid with haptogenic properties is cardiolipin. The question whether this haptogenic property is due to the free OH-group remains to be answered. 

Hoffmann 161) and Hoffmann and Rapport 162) reported the solubilization and purification of specific DPN and TPN cleaving enzymes from rabbit erythrocytes. These enzymes are inhibited by nicotinamide this inhibition is competitive in contrast to the noncompetitive inhibition shown by the beef spleen and pig brain enzymes. It has also been reported that the rabbit erythrocyte enzymes do not act as trani ycosidases. It has been found that the DPNases in nearly all mammalian tissues, even when purified, are both hydrolases and transglycosidases, that they show a noncompetitive inhibition with nicotinamide, and that they act almost equally well on both DPN and TPN 16S, 164)- The erythrocyte enzymes may be different types of enzymes however, it has been shown that in human erythrocytes the same enzyme splits both DPN and TPN 165). In bull seminal fluid, the DPNase and TPNase activities appear to be due to separate entities 166). 

Glycosphingolipids derived from series III, which show blood group activity in the A, B, O (H), Le , Le - system, were observed by Hakomori and Strycharz (1968) and Hakomori and Andrews (1970). A blood group B active oligohexosyl ceramide was isolated from rabbit erythrocytes and the following structure proposed (Eto et al., 1968) ... 

A number of polyacrylamide gel electrophoreses from fraction I were run and not fixed and stained. At the position of the enzyme peak in parallel gels appropriate slices were cut out, macerated, mixed with Freund s adjuvant and used to immunize a rabbit. The antiserum obtained had a low titer but inhibited the activity of all 3 isoenzymes. It did not crossreact with HGPRT from rabbit or human erythrocytes. 

Figure 4. Neutralization of erythrocyte PP-ribose-P synthetase activity by concentrated serum IgG from rabbits immunized with purified normal PP-ribose-P synthetase. To a constant amount of erythrocyte extract, increasing amounts of antiserum were added and after incubation at 37° and 4° each for 30 minutes, enzyme activity was measured. Enzyme from erythrocytes of... 

Complement activity was first recognized by Bordet, who showed that the lytic activity of rabbit anti-sheep erythrocyte serum was lost on heating to 56°C but was restored by the addition of fiesh serum from an unimmunized rabbit. Thus, two faetors were necessary, a heat-stable factor, antibody, plus a heat-labile factor, complement, whieh is present in all sera. 

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