THE METABOLISM OF THE ERYTHROCYTE: XI SYNTHESIS OF DIPHOSPHOPYRIDINE NUCLEOTIDE IN THE ERYTHROCYTE

1956 ◽  
Vol 34 (2) ◽  
pp. 130-140 ◽  
Author(s):  
A. Malkin ◽  
O. F. Denstedt
Keyword(s):  
Particulate Fraction ◽  
Cell Nuclei ◽  
Chicken Erythrocytes ◽  
Rabbit Reticulocytes

DPN pyrophosphorylase activity has been demonstrated in chicken erythrocytes, but could not be found in rabbit reticulocytes nor in human or rabbit erythrocytes. In the erythrocyte of the chicken, the activity was confined to the particulate fraction, which consists mainly of cell nuclei. The implications of these findings with respect to the maturation of the erythrocyte and the metabolic interrelationship between the nucleus and the cytoplasm are discussed.

THE METABOLISM OF THE ERYTHROCYTE: XI SYNTHESIS OF DIPHOSPHOPYRIDINE NUCLEOTIDE IN THE ERYTHROCYTE

1956 ◽  
Vol 34 (1) ◽  
pp. 130-140 ◽  
Author(s):  
A. Malkin ◽  
O. F. Denstedt
Keyword(s):  
Particulate Fraction ◽  
Cell Nuclei ◽  
Chicken Erythrocytes ◽  
Rabbit Reticulocytes

DPN pyrophosphorylase activity has been demonstrated in chicken erythrocytes, but could not be found in rabbit reticulocytes nor in human or rabbit erythrocytes. In the erythrocyte of the chicken, the activity was confined to the particulate fraction, which consists mainly of cell nuclei. The implications of these findings with respect to the maturation of the erythrocyte and the metabolic interrelationship between the nucleus and the cytoplasm are discussed.

CYTOCHROME OXIDASE ACTIVITY OF CELL NUCLEI

1954 ◽  
Vol 32 (1) ◽  
pp. 548-552 ◽  
Author(s):  
David Rubinstein ◽  
Orville F. Denstedt
Keyword(s):  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Nuclear Material ◽  
Liver Cells ◽  
Nuclear Fraction ◽  
Cell Nuclei ◽  
Nuclear Membranes ◽  
Rat Liver Cells ◽  
Chicken Erythrocytes

The presence of cytochrome oxidase in the nuclear material from chicken erythrocytes and rat-liver cells has been demonstrated with the aid of p-phenylenediamine as the agent for reducing cytochrome c. The three reagents p-phenylenediamine, ascorbate, and hydroquinone are effective in the estimation of cytochrome oxidase in mitochondrial preparations, but only the first mentioned agent can effect the reduction of endogenous cytochrome c. The addition of cytochrome c will increase the oxidase activity of the liver-cell mitochondria but not of the nuclear fraction from the erythrocytes or the liver cells, presumably because of the impermeability of the nuclear membranes to added cytochrome c.

CYTOCHROME OXIDASE ACTIVITY OF CELL NUCLEI

1954 ◽  
Vol 32 (5) ◽  
pp. 548-552 ◽  
Author(s):  
David Rubinstein ◽  
Orville F. Denstedt
Keyword(s):  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Nuclear Material ◽  
Liver Cells ◽  
Nuclear Fraction ◽  
Cell Nuclei ◽  
Nuclear Membranes ◽  
Rat Liver Cells ◽  
Chicken Erythrocytes

The presence of cytochrome oxidase in the nuclear material from chicken erythrocytes and rat-liver cells has been demonstrated with the aid of p-phenylenediamine as the agent for reducing cytochrome c. The three reagents p-phenylenediamine, ascorbate, and hydroquinone are effective in the estimation of cytochrome oxidase in mitochondrial preparations, but only the first mentioned agent can effect the reduction of endogenous cytochrome c. The addition of cytochrome c will increase the oxidase activity of the liver-cell mitochondria but not of the nuclear fraction from the erythrocytes or the liver cells, presumably because of the impermeability of the nuclear membranes to added cytochrome c.

Subcellular site of porphyrin biosynthesis in nucleated erythrocytes

1965 ◽  
Vol 208 (6) ◽  
pp. 1270-1274 ◽  
Author(s):  
Vishwanath M. Sardesai ◽  
Sally A. Doehr ◽  
James M. Orten
Keyword(s):  
Liver Cell ◽  
Aminolevulinic Acid ◽  
Subcellular Fractions ◽  
Particulate Fraction ◽  
Supernatant Fraction ◽  
Intact Cells ◽  
Cellular Fraction ◽  
Chicken Erythrocytes

The activity of hemolysates, prepared by several different methods from nucleated (chicken) erythrocytes, and of their subcellular fractions in forming porphyrins from glycine plus acetate or succinate or from δ-aminolevulinic acid (ALA) was studied. In general, hemolysates were less active than intact cells in porphyrin biosynthesis from glycine and acetate but were more active with ALA as the substrate. The supernatant fraction formed coproporphyrin from ALA but not from glycine and acetate. Protoporphyrin was not formed from either precursor by the supernatant fraction. The particulate fraction alone was devoid of porphyrin-forming activity, and also of ALA- and porphobilinogen- (PBG) forming activity. The combined particulate-supernatant fractions, however, synthesized both copro- and protoporphyrins from either glycine and acetate or ALA, but of course more from the latter. Dialysis or heating to 60 C destroyed the activity of the supernatant. These results indicate that "compartmentation" of porphyrin biosynthesis occurs in the nucleated erythrocyte much as in the liver cell, the step from ALA to coproporphyrinogen being carried out in the soluble, "nonparticulate" cellular fraction and the remaining steps in the "particulate" fraction.

scholarly journals Genome size of the European domestic goose (Anser anser domesticus)

2009 ◽  
Vol 89 (4) ◽  
pp. 449-455 ◽  
Author(s):  
K Andraszek ◽  
E Wójcik ◽  
A Grużewska ◽  
E Smalec
Keyword(s):  
Genome Size ◽  
Dna Content ◽  
Cell Types ◽  
Heart Cells ◽  
Feulgen Reaction ◽  
Cell Nuclei ◽  
Anser Anser ◽  
Ovary Cells ◽  
Nucleus Surface ◽  
Chicken Erythrocytes

This work is aimed at determining the C-DNA contained within the nuclei of different types of cells in the domestic goose Anser anser. Cells from the lungs, skin, pancreas, kidney, spleen, liver, heart, brain, blood, ovary and testicle were analysed. Cells from the blood, ovary and testicle were smeared onto microscopic glasses, whereas slides from the other organs and tissues were prepared using the paraffin technique. DNA content, as visualized by the Feulgen reaction using computerized image analysis, was examined in 200 nuclei of every type of cell. Chicken erythrocytes were used as reference material. Different concentrations of chromatin within cell nuclei were observed, from small, dispersed clods to an entirely filled nucleus surface. It was stated that the average C-DNA content in the domestic European goose amounts to 1.306 ± 0.327 pg, which gives goose DNA a length in base pair of 1.277 × 109 ± 0.320 × 109 bp after adjustment. The correlation between nucleus size and the C-DNA content was positive and high. In all cell types it exceeded 0.6. The highest was observed in lung and ovary cells, the lowest in skin and the pancreas. The majority of all cells (57.34%) contain DNA at the range between 1.0 to 1.5 pg, especially those from erythrocytes and the pancreas (82 and 76% respectively). Liver cells demonstrate a tendency toward an amount that is higher than 1.5% of the DNA (78.61% cells). Heart cells reveal a tendency downward (98.99% below 1.5 pg). Less than 1.0 pg of DNA was observed in 17.13% of all examined cells. Key words: Domestic goose, cell, cell nuclei, Feulgen reaction, genome size, DNA mass

Variability in cell-specific and common histones of avian erythrocytes

1968 ◽  
Vol 46 (3) ◽  
pp. 241-247 ◽  
Author(s):  
J. M. Neelin
Keyword(s):  
Conformational Changes ◽  
Electrophoretic Pattern ◽  
Acid Extraction ◽  
Red Cell ◽  
Cell Nuclei ◽  
Tissue Specific ◽  
Physiological Conditions ◽  
Avian Erythrocytes ◽  
Chicken Erythrocytes ◽  
Characteristic Component

Histones extracted with acid from duck, goose, turkey, pigeon, and gull erythrocyte nuclei contained a major component, electrophoretically homologous with the serine-rich histone of chicken erythrocytes. This characteristic component was lacking or adventitious in duck, goose, and turkey spleens and marrows (as well as chicken tissues), but prominent in erythrocytes from birds under various physiological conditions, in reticulocytes as well as mature erythrocytes, and in nuclei prepared under various circumstances of cytolysis.Other electrophoretic components of erythrocytes and tissues, some apparently tissue-specific, were more variable in occurrence. Electrophoretic zones corresponding to arginine-rich histones, which had previously been considered as specifically absent from chicken erythrocytes, were in fact especially refractory to acid extraction from red cell nuclei. Furthermore, variability in electrophoretic pattern of these zones was attributed in part to conformational changes, which were sensitive to β-mercaptoethanol and to urea.

Intranuclear Crystals in Regenerating Canine Kidneys

1973 ◽  
Vol 31 ◽  
pp. 412-413
Author(s):  
D.G. Osborne ◽  
L.J. McCormack ◽  
M.O. Magnusson ◽  
W.S. Kiser
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Tubular Epithelial Cell ◽  
Tubular Epithelial Cells ◽  
Cell Nuclei ◽  
Crystalline Structures ◽  
Small Crystals ◽  
Membrane Bound

During a project in which regenerative changes were studied in autotransplanted canine kidneys, intranuclear crystals were seen in a small number of tubular epithelial cells. These crystalline structures were seen in the control specimens and also in regenerating specimens; the main differences being in size and number of them. The control specimens showed a few tubular epithelial cell nuclei almost completely occupied by large crystals that were not membrane bound. Subsequent follow-up biopsies of the same kidneys contained similar intranuclear crystals but of a much smaller size. Some of these nuclei contained several small crystals. The small crystals occurred at one week following transplantation and were seen even four weeks following transplantation. As time passed, the small crystals appeared to fuse to form larger crystals.

The structure of pre-mRNA and mRNA from erythroid cells

1978 ◽  
Vol 36 (2) ◽  
pp. 234-235
Author(s):  
A.-M. Ladhoff ◽  
B.J. Thiele ◽  
Ch. Coutelle ◽  
S. Rosenthal
Keyword(s):  
Bone Marrow ◽  
Structural Transformation ◽  
Electron Micrographs ◽  
Ammonium Acetate ◽  
Bone Marrow Cells ◽  
Erythroid Cells ◽  
Globin Mrna ◽  
Ordered Structures ◽  
Rabbit Bone ◽  
Rabbit Reticulocytes

The suggested precursor-product relationship between the nuclear pre-mRNA and the cytoplasmic mRNA has created increased interest also in the structure of these RNA species. Previously we have been published electron micrographs of individual pre-mRNA molecules from erythroid cells. An intersting observation was the appearance of a contour, probably corresponding to higher ordered structures, on one end of 10 % of the pre-mRNA molecules from erythroid rabbit bone marrow cells (Fig. 1A). A virtual similar contour was observed in molecules of 9S globin mRNA from rabbit reticulocytes (Fig. 1B). A structural transformation in a linear contour occurs if the RNA is heated for 10 min to 90°C in the presence of 80 % formamide. This structural transformation is reversible when the denatured RNA is precipitated and redissolved in 0.2 M ammonium acetate.

Three-dimensional reconstruction of the 40S ribosomal subunit from rabbit reticulocytes

1987 ◽  
Vol 45 ◽  
pp. 936-937
Author(s):  
Neng-Yu Zhang ◽  
Terence Wagenknecht ◽  
Michael Radermacher ◽  
Tom Obrig ◽  
Joachim Frank
Keyword(s):  
Three Dimensional ◽  
Ribosomal Subunit ◽  
Uranyl Acetate ◽  
Reconstruction Method ◽  
Single Exposure ◽  
Electron Dose ◽  
Ribosomal Subunits ◽  
40S Ribosomal Subunit ◽  
Dimensional Reconstruction ◽  
Rabbit Reticulocytes

We have reconstructed the 40S ribosomal subunit at a resolution of 4 nm using the single-exposure pseudo-conical reconstruction method of Radermacher et al.Small (40S) ribosomal subunits were Isolated from rabbit reticulocytes, applied to grids and negatively stained (0.5% uranyl acetate) in a manner that “sandwiches” the specimen between two layers of carbon. Regions of the grid exhibiting uniform and thick staining were identified and photographed twice (magnification 49,000X). The first micrograph was always taken with the specimen tilted by 50° and the second was of the Identical area untilted (Fig. 1). For each of the micrographs the specimen was subjected to an electron dose of 2000-3000 el/nm2.Three hundred thirty particles appearing in the L view (defined in [4]) were selected from both tilted- and untilted-specimen micrographs. The untilted particles were aligned and their rotational alignment produced the azimuthal angles of the tilted particles in the conical tilt series.

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