Avian erythrocytes

B2. Barron, E. S. G., and Harrop, G. A., The effect of methylene blue and other dyes upon the glycolysis and lactic acid formation of mammalian and avian erythrocytes. J. Biol. Chetn. 79, 65-87 (1028). 

HI forms a microheterogeneous group of very lysine-rich histones. In nucleated avian erythrocytes H5 is also present (for references, see Cole, 1977), bearing a similarity in sequence and stoichiometry to HI. Histone HI does not interact with the other core histones in solution... 

Georgatos, S. D., and Blobel, G. (1987b). Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes A basis for a vectorial assembly of intermediate filaments./. Biol. Chem. 105, 105-115. 

Granger, B. L., and Lazarides, E. (1982). Structural association of synemin and vimentin in avian erythrocytes revealed by immunoelectron microscopy. Cell 30, 263-275. 

Moss J, Stanley SJ, Oppenheimer NJ (1979a) Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes. In J. Biol. Chem. 255 7835-7837. 

Moss J, Vaughan M (1978) Isolation of an avian erythrocyte protein possessing ADP-ribosyltransferase activity and capable of activating adenylate cyclase. In Proc. Natl. Acad. Sci. USA 75 3621 -3624. 

The type I enzyme from avian erythrocytes has also been shown to perform intermolecular strand transfer (Trask and Muller, 1983). 

Inositol (hexahydroxycyclohexane) occurs in several isomeric forms. Myo-inositol (or meso-inositol) is an important constituent of phospholipids and is the only isomer with biological activity. Inositol hexaphosphate (phytic acid) is found in avian erythrocytes, where it binds to hemoglobin, thereby regulating the oxygen capacity of the blood. It is also important as an intracellular messenger in a number of pathways. 

All animal cells studied up to now show the abiUty to accumulate certain amino acids against their concentration gradients, while for sugars such accumulation was only observed in polarized cells, e.g. cells from small intestine or proximal tubule. Ehrlich cells and other tumor cell lines [53-57], tissue culture cells, avian erythrocytes [58], isolated cells and slices from different tissues [59] were studied for their ability to accumulate amino acids. Apart from investigations with epithelia, studies, on Ehrlich cells, of the energetics and mechanism of the accumulative uptake of amino acids play a fundamental role in working out the concept of cotransport between Na and amino acids by animal cells. 

Erythrocytes are unusual compared with other tissues in that there is little turnover during the lifetime of the cell, and the proteins become degraded when the cell itself is degraded. In humans, erythrocytes have an average life of 120 days, whereas avian erythrocytes have an average life of 35 days. The principal protein in erythrocytes is haemoglobin. 

Although both these processes occur in mammalian erythrocytes, only the first effect occurs in avian erythrocytes. This is apparent because the magnitude of the effect of carbon choxide on avian haemoglobin is the same as that with any other acid and is thus through [H ] alone (Maginniss, 1985). This difference... 

Isaacks, R.E., Harkness, D.R., Sampsell, R.N., Adler, J.L., Kim, C.Y. Goldman, P.H. (1976). Studies on avian erythrocyte metabolism-IV. Relationship between the major phos-phorylated metabolic intermediates and oxygen affinity of whole blood in adults and embryos in several Galliformes. Comp. Biochem. Physiol, 5 5A, 29—33. 

Isaacks, R.E., Kim, C., Liu, H.L., Goldman, P., Johnsoa A. Harkness, D. (1983). Studies on avian erythrocyte metabolism. XIII. Changing organic phosphate composition in age-dependent density populations of chicken erythrocytes. Poult. Sci., 62, 1639- 6. 

Ruiz-Larrea, F. Berrie, CP. (1993). Characterization of a membrane-associated, receptor and G-protein responsive phosphoinositide-specific phospholipase C from avian erythrocytes. FEBS Lett., 328, 174-82. 

Sodium phosphate provides excellent buffering for fixatives at 0.1 M and is often used in place of cacodylate. Each buffer system has certain advantages and limitations. Cacodylate is an organic arsenic compound, dimethylarsenate, which is poisonous. Whereas it may provide additional TEM contrast in biological samples, it is a relatively weak buffer at pH 7.2. Alternatively, phosphate requires fewer safety precautions. However, our laboratory has observed precipitants in some biological samples, such as avian erythrocytes, that were attributed to the phosphate buffer. 

High quality, high molecular weight genomic DNA is essential for successful DNA fingerprint analysis, and is conveniently prepared from avian erythrocytes. For mammalian studies DNA is usually prepared from isolated leucocytes, alternatively homogenized tissues may be used (e.g. liver). 

The structure of some universal polyols can also be confirmed by NMR techniques, involving and P NMR. myo-Inositol-l,3,4,5,6-pentakisphosphate has been identified by these techniques in avian erythrocytes after separation of inositol polyphosphates by Dowex 1x2 chromatography. Arabitol, mannitol, and ribitol have also been identified using natural abundance criteria by NMR spectroscopy in a number of lichen species. 

SDS-polyacrylamide gel electrophoresis. The substrate specificity was rather loose with the protein portion ADP-ribosyl histones HI and H2B, peptide fragments of H2B, and nonhistone proteins (a mixture) served as substrates. In contrast, the specificity was very tight with the mono(ADP-ribosyl) portion and the carboxyl ester bond poly- or oligo(ADP-ribosyl) histones were hardly split, and ADP-ribose histone adducts formed chemically through Schiff base reduction [3] or ADP-ribosyl arginine bond formed by avian erythrocyte ADP-ribosyltransferase [14] did not serve as substrate. 

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