The Avian Erythrocyte

2016 ◽  
Author(s):  
Chester A. Glomski ◽  
Alessandra Pica
Keyword(s):  
Avian Erythrocyte

scholarly journals Only a small fraction of avian erythrocyte histone is involved in ongoing acetylation

1981 ◽  
Vol 9 (19) ◽  
pp. 5061-5074 ◽  
Author(s):  
T.W. Brotherton ◽  
J. Covault ◽  
A. Shires ◽  
R. Chalkley
Keyword(s):  
Avian Erythrocyte

Studies on avian erythrocyte metabolism

1987 ◽  
Vol 257 (1) ◽  
pp. 177-185 ◽  
Author(s):  
R.E. Isaacks ◽  
L.L. Lai ◽  
P.H. Goldman ◽  
C.Y. Kim
Keyword(s):  
Avian Erythrocyte ◽  
Erythrocyte Metabolism

Restriction of RNA Synthesis by RNA Polymerase from Avian Erythrocyte Nuclei

1974 ◽  
pp. 295-302 ◽  
Author(s):  
R. K. Mandal ◽  
Hemanta K. Mazumder ◽  
B. B. Biswas
Keyword(s):  
Rna Polymerase ◽  
Rna Synthesis ◽  
Avian Erythrocyte

Studies on avian erythrocyte metabolism

1980 ◽  
Vol 75 (2) ◽  
pp. 485-491 ◽  
Author(s):  
R.E. Isaacks ◽  
C.Y. Kim ◽  
T.J. Legato ◽  
A.E. Johnson ◽  
P.H. Goldman ◽  
...  
Keyword(s):  
Avian Erythrocyte ◽  
Erythrocyte Metabolism

A modified fractionation procedure for avian erythrocyte histones

1969 ◽  
Vol 47 (12) ◽  
pp. 1121-1123 ◽  
Author(s):  
G. H. M. Adams ◽  
J. M. Neelin
Keyword(s):  
Cation Exchange ◽  
Exchange Chromatography ◽  
Cation Exchange Chromatography ◽  
Fractionation Procedure ◽  
Exclusion Chromatography ◽  
One Step ◽  
Avian Erythrocyte ◽  
Fractionation Method ◽  
Time Required

The fractionation method of Vidali and Neelin for avian erythrocyte histones was modified to reduce the time required to obtain clean fractions of serine-rich and arginine-rich histones. Histones were extracted from washed nuclei in one step with 0.20 M HCl. The lysine-rich and the moderately lysine-rich histones were fractionated by cation-exchange chromatography but the serine-rich and arginine-rich histones were eluted together. These histones were separated by subsequent exclusion chromatography.

The preparation and ultrastructure of avian erythrocyte nuclear envelope enclosed by the plasma membrane

1978 ◽  
Vol 34 (1) ◽  
pp. 81-90
Author(s):  
J.R. Harris
Keyword(s):  
Plasma Membrane ◽  
Nuclear Envelope ◽  
Ammonium Molybdate ◽  
Negative Staining ◽  
Nuclear Pore ◽  
Nuclear Pore Complexes ◽  
Thin Sectioning ◽  
Avian Erythrocyte ◽  
Pore Complexes ◽  
Low Ionic Strength

A procedure is described for the preparation of avian erythrocyte nuclear envelope ghosts which remain enclosed by the ellipsoid plasma membrane. Haemoglobin-free nucleated chicken erythrocyte ghosts are treated in a low ionic strength buffer plus heparin which brings about decondensation of the chromatin. This is followed by solubilization of the chromatin by digestion with pancreatic deoxyribonuclease-1. When studied by light microscopy using either phase-contrast or Nomarski interference optics, the ellipsoid plasma membrane is clearly seen to remain with the collapsed nuclear envelope trapped inside. This interpretation is supported by negative-staining electron microscopy using ammonium molybdate, which in addition reveals the presence of the nuclear pore complexes. The suggestion is advanced that structural protection is provided for the fragile nuclear envelope system by the surrounding plasma membrane, which might account for the final nuclear envelope being in the form of relatively intact ghosts with well defined nuclear pore complexes. The nuclear envelope is highly fragmented when the plasma membrane is absent, the nuclear pore complexes showing appreciable breakdown. Thin sectioning supports the results of negative staining and in addition shows the nuclear envelope retained within the plasma membrane to be composed of both inner and outer nuclear membranes, but the nuclear pore complexes are not clearly defined.

Effect of Reserpine Pretreatment on Avian Erythrocyte Carbonic Anhydrase Activation by Isoproterenol

Pharmacology ◽  
1994 ◽  
Vol 49 (2) ◽  
pp. 112-120 ◽  
Author(s):  
Immaculata N.A. Igbo ◽  
Charles E. Reigel, Jr. ◽  
Ingrid M. Greene ◽  
Alexander D. Kenny
Keyword(s):  
Carbonic Anhydrase ◽  
Avian Erythrocyte ◽  
Erythrocyte Carbonic Anhydrase

The stability of acid-soluble chromosomal proteins from avian erythrocytes

1968 ◽  
Vol 46 (8) ◽  
pp. 781-788 ◽  
Author(s):  
G. Vidali ◽  
J. M. Neelin
Keyword(s):  
Acetic Acid ◽  
Room Temperature ◽  
Starch Gel Electrophoresis ◽  
Guanidinium Chloride ◽  
Chromosomal Proteins ◽  
Avian Erythrocytes ◽  
Starch Gel ◽  
Avian Erythrocyte ◽  
The Stability ◽  
And Storage

The stability of avian erythrocyte histones was examined under the conditions of extraction, chromatography, electrophoresis, and storage, in order to avoid degradation during these operations. Since turbidity in trichloroacetic acid (TCA) was used as a measure of histone integrity, optimal conditions for quantitative assay were established as follows. One volume of histone sample was mixed with five volumes of 1.1 M TCA at room temperature, and the optical density at 400 mμ was measured after 25 min. The relation between turbidity and protein concentration was linear from 0.03 to at least 0.3 mg histone per milliliter and was not related to the kind of histone, except for the lysine-rich fraction which showed slightly less specific turbidity. Under these conditions turbidity was not sensitive to concomitant solutes such as guanidinium chloride, acetic acid, and dilute buffers and acids.With turbidity as the criterion of protein integrity, it was confirmed that brief manipulation in the cold is desirable in most media, including the dilute acids used for extraction. Nevertheless, chromatography at room temperature in concentrated solutions of guanidinium chloride or acetic acid appears to be tolerably safe. The effect of these conditions of manipulation and storage on histone fractions was substantiated by chromatography and starch-gel electrophoresis. Prolonged extraction of avian erythrocyte nuclei at acid pH released additional non-histone basic protein without alteration of authentic histone fractions.

scholarly journals The Transfusion Behavior of Avian Erythrocytes: The Lack of Functional Transplantation Antigens in a Nucleated Cell

Blood ◽  
1961 ◽  
Vol 18 (2) ◽  
pp. 207-219 ◽  
Author(s):  
ROBERT SILBER ◽  
STEPHEN E. HEDBERG ◽  
JOSEPH H. AKEROYD ◽  
DONALD FELDMAN
Keyword(s):  
Blood Group ◽  
Blood Groups ◽  
Naturally Occurring ◽  
Apparent Relationship ◽  
Avian Erythrocytes ◽  
Avian Erythrocyte ◽  
Compatible Blood ◽  
Transplantation Antigens

Abstract 1. Autotransfusion and cross-transfusion experiments in the turkey reveal that the avian erythrocyte, despite the presence of a nucleus, survives normally in homologous recipients of compatible blood groups. 2. Skin homografts were rejected without apparent relationship to blood group compatibility. 3. Evidence for blood groups in the turkey is presented. While no naturally occurring iso-agglutinins were found, stimulation led to the appearance of incomplete antibodies.

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