scholarly journals UPTAKE OF GLYCINE-N15 BY COMPONENTS OF CELL NUCLEI

1952 ◽  
Vol 36 (2) ◽  
pp. 173-179 ◽  
Author(s):  
Marie M. Daly ◽  
V. G. Allfrey ◽  
A. E. Mirsky
Keyword(s):  
Metabolic Rates ◽  
Cytoplasmic Protein ◽  
Cell Nuclei ◽  
Residual Protein ◽  
Avian Erythrocytes ◽  
Mammalian Liver

1. The uptake of glycine-N15 by components of cell nuclei was studied. The nuclear components were derived both from tissues with high metabolic rates-mammalian liver, kidney, and pancreas-and from cells with relatively low rates of metabolism-avian erythrocytes and echinoderm sperm. N15 uptake by nuclear components of liver, kidney, and pancreas was far more rapid than by those of erythrocytes and sperm. 2. The nuclear components of liver, kidney, and pancreas for which measurements were made were DNA, histone, and residual protein of chromatin. Uptake into DNA was low, into histone higher, and into residual protein much higher still, being comparable with that into mixed cytoplasmic protein. 3. A comparison of the uptake of N15 by the chromosomal components, histone and DNA of liver, pancreas, and kidney showed that chromosomal "activity" varies in different cells and also in the same cell depending upon its over-all activity.

Further studies of DNA-nucleoprotein gels and residual protein of isolated cell nuclei

1968 ◽  
Vol 49 (3) ◽  
pp. 533-557 ◽  
Author(s):  
M. Mackay ◽  
C.A. Hilgartner ◽  
A.L. Dounce
Keyword(s):  
Cell Nuclei ◽  
Residual Protein ◽  
Isolated Cell

scholarly journals THE ISOLATION OF CELL NUCLEI IN NON-AQUEOUS MEDIA

1952 ◽  
Vol 35 (3) ◽  
pp. 529-557 ◽  
Author(s):  
V. Allfrey ◽  
H. Stern ◽  
A. E. Mirsky ◽  
H. Saetren
Keyword(s):  
Citric Acid ◽  
Serum Proteins ◽  
Aqueous Media ◽  
Organic Media ◽  
Cell Nuclei ◽  
Intracellular Enzyme ◽  
Cytoplasmic Proteins ◽  
Immunological Tests ◽  
Avian Erythrocytes ◽  
Enzyme Distribution

1. A modified Behrens procedure is described for the isolation of nuclei from avian erythrocytes and from the liver, kidney, thymus, pancreas, heart, and intestinal mucosa of the calf or horse. 2. The purity of these nuclei has been established by staining reactions, enzyme studies, and immunological tests for serum proteins. 3. Evidence is presented to show that a transport of cytoplasmic proteins into the nucleus does not occur during the isolation. 4. Nuclei prepared in non-aqueous media contain considerably more protein and a very different enzyme composition from that observed in nuclei prepared by "homogenization" techniques in dilute citric acid. 5. The suitability of nuclei prepared in organic media for the study of intracellular enzyme distribution is discussed.

scholarly journals ACTION OF MITOCHONDRIAL DNAASE I IN DESTROYING THE CAPACITY OF ISOLATED CELL NUCLEI TO FORM GELS

1957 ◽  
Vol 3 (5) ◽  
pp. 649-662 ◽  
Author(s):  
Alexander L. Dounce ◽  
Marguerite P. O'Connell ◽  
Kenneth J. Monty ◽  
Keyword(s):  
Rat Liver ◽  
Enzyme System ◽  
Sodium Dodecyl ◽  
Detergent Solution ◽  
Cell Nuclei ◽  
Ph Values ◽  
Residual Protein ◽  
Mitochondria Dna ◽  
Liver Nuclei ◽  
Isolated Cell

1. DNA prepared from non-gelable rat liver nuclei isolated in the presence of disrupted mitochondria at pH 6.0, has been compared with DNA obtained from gelable nuclei isolated at pH 4.0. The DNA of the non-gelable nuclei is partially depolymerized relative to the DNA of the gelable nuclei. 2. It has been found that sufficiently small quantities of crystallized DNAase I can cleave a very large part of the DNA of gelable nuclei isolated at pH 4 from the residual protein of these nuclei without causing extensive depolymerization of the DNA. At the same time the gelable nuclei are rendered non-gelable. 3. Partially purified DNAase II can also render gelable nuclei isolated at pH 4 non-gelable, and in so doing presumably also cleaves the DNA from the residual protein of the nuclei. 4. Mitochondrial DNAase I appears to be the enzyme responsible to a large extent for the cleavage of DNA from the residual protein of gelable rat liver cell nuclei with concomitant destruction of the gel-forming capability of these nuclei, when the nuclei are subjected to the action of disrupted mitochondria at pH 6.0 during the isolation procedure. 5. Mitochondrial DNAase II does not appear to exert appreciable action on nuclei during the course of isolation of the nuclei at pH 6.0 in the presence of disrupted mitochondria. 6. It is probable that DNAase I is not the sole enzyme responsible for destroying the gelability of nuclei isolated at pH 6.0 in the presence of disrupted mitochondria. Protease may be involved. 7. Sodium dodecyl sulfate at pH 6.0–6.3 cleaves the DNA of isolated gelable nuclei from the residual protein of these nuclei over a period of 2 to 3 hours. At pH 7.0–7.5, however, there is negligible cleavage over a period of 96 hours. 8. If non-gelable nuclei are isolated at pH 6.0 in the presence of disrupted mitochondria, DNA subsequently can be removed from them by the use of detergent at pH values ranging from 6.0–7.5 without the necessity of incubation in the detergent solution, since the DNA had already been detached from the residual protein by the action of the mitochondrial enzyme system during isolation of the nuclei.

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.

Quality control of washed red blood cells: experience in determining residual protein

2020 ◽  
Vol 1 ◽  
pp. 65-67
Author(s):  
O.V. Kozhemyako ◽  
◽  
Ya.E. Zhigalina ◽  
E.L. Zeiler ◽  
L.V. Golovanova ◽  
...  
Keyword(s):  
Quality Control ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Residual Protein

Enzymic Correlates of Development, Secretory Function and Regression of Follicles and Corpora Lutea in the Bovine Ovary. PART II: Formation, Development and Involution of Corpora Lutea

1968 ◽  
Vol 59 (2_Suppl) ◽  
pp. S35-S51 ◽  
Author(s):  
B. L. Lobel ◽  
E. Levy
Keyword(s):  
Corpus Luteum ◽  
Vascular System ◽  
Hydrolytic Enzymes ◽  
Sharp Decrease ◽  
Cellular Growth ◽  
Corpora Lutea ◽  
Cell Nuclei ◽  
Steroid Synthesis ◽  
Luteal Cells ◽  
Vascular Walls

ABSTRACT Activities of various hydrolases and dehydrogenases were studied during the formation, development and involution of cyclic corpora lutea and in the corpora lutea of early pregnancy. At 24 hours postovulation the luteal cells, whether of granulosal or thecal origin, contained demonstrable levels of Δ5-3β-hydroxysteroid dehydrogenase and the NADP and NADPH2 diaphorases. During the period of proliferation and cellular growth, enzymic activities in the luteal cells were moderate at first, and then increased. In the mature corpus luteum, activities of the dehydrogenases occurred in all luteal cells but were most intense in the large polymorphic luteal cells. Activities of hydrolytic enzymes, low in the immediate postovulatory period, increased with the development of the vascular system. Enzymic characteristics of corpora lutea of gestation were similar to those of cyclic corpora, except for phosphorylase activity which was observed in luteal cells in gestational corpora, but confined to the vascular walls in cyclic corpora. No increase in activities of 17β- and 20β-hydroxysteroid dehydrogenases (above those seen in pre-ovulatory follicles) were observed after incubation of sections of either mature cyclic or gestational corpora. Involution of cyclic corpora lutea began with degenerative changes in the blood vessels: pyknosis of the endothelial cell nuclei and a sudden decline in activities of hydrolytic enzymes in the vascular walls. Subsequently, the luteal cells showed a sharp decrease in activities of the dehydrogenases as well as other signs of regressive change. The cytochemical findings are discussed in relation to biochemical observations on steroid synthesis by the bovine corpus luteum.

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