scholarly journals Effect of erythropoietin on chromosomal protein synthesis

Blood ◽  
1976 ◽  
Vol 47 (4) ◽  
pp. 581-592 ◽  
Author(s):  
JL Spivak
Keyword(s):  
Isotope Labeling ◽  
Specific Activity ◽  
Splenic Tissue ◽  
Chromosomal Protein ◽  
Histone Proteins ◽  
Total Histone ◽  
Chromosomal Proteins ◽  
Nonhistone Protein ◽  
The Individual ◽  
Double Isotope

Abstract The spleen of the exhypoxic polycythemic mouse was employed to study the effect of erythropoietin on the synthesis of chromosomal proteins. At 1, 3, 18, 36, 45, and 72 hr after injection of erythropoietin, spleens were removed, minced, and incubated with 3H-arginine for 1 hr. Chromatin was isolated from the labeled splenic tissue and separated into histone and nonhistone protein (NHP) fractions. An increase in the incorporation of 3H-arginine into NHP occurred within 3 hr and into histones by 18 hr. Incorporation of 3H-arginine into both histones and NHP was maximal by 45 hr and had declined by 72 hr. Total histone specific activity increased fivefold while NHP specific activity increased twofold. Histones and NHP were fractionated on polyacrylamide gels and a double isotope labeling proceudre was used to study the synthesis of the individual histone proteins and NHP. Following administration of erythropoietin, there was a coordinate increase in the specific activity of all five major histone proteins and most of the NHP. The earliest change in specific activity of both histones and NHP occurred prior to the appearance of morphologically identifiable erythroblasts in the spleen.

scholarly journals Effect of erythropoietin on chromosomal protein synthesis

Blood ◽  
1976 ◽  
Vol 47 (4) ◽  
pp. 581-592
Author(s):  
JL Spivak
Keyword(s):  
Isotope Labeling ◽  
Specific Activity ◽  
Splenic Tissue ◽  
Chromosomal Protein ◽  
Histone Proteins ◽  
Total Histone ◽  
Chromosomal Proteins ◽  
Nonhistone Protein ◽  
The Individual ◽  
Double Isotope

The spleen of the exhypoxic polycythemic mouse was employed to study the effect of erythropoietin on the synthesis of chromosomal proteins. At 1, 3, 18, 36, 45, and 72 hr after injection of erythropoietin, spleens were removed, minced, and incubated with 3H-arginine for 1 hr. Chromatin was isolated from the labeled splenic tissue and separated into histone and nonhistone protein (NHP) fractions. An increase in the incorporation of 3H-arginine into NHP occurred within 3 hr and into histones by 18 hr. Incorporation of 3H-arginine into both histones and NHP was maximal by 45 hr and had declined by 72 hr. Total histone specific activity increased fivefold while NHP specific activity increased twofold. Histones and NHP were fractionated on polyacrylamide gels and a double isotope labeling proceudre was used to study the synthesis of the individual histone proteins and NHP. Following administration of erythropoietin, there was a coordinate increase in the specific activity of all five major histone proteins and most of the NHP. The earliest change in specific activity of both histones and NHP occurred prior to the appearance of morphologically identifiable erythroblasts in the spleen.

STUDIES ON THYROIDAL COLLOID PINOCYTOSIS USING A DOUBLE ISOTOPE TECHNIQUE

1972 ◽  
Vol 70 (1) ◽  
pp. 48-55 ◽  
Author(s):  
Mario A. Pisarev ◽  
Noe Altschuler ◽  
Leslie J. DeGroot
Keyword(s):  
Acid Phosphatase ◽  
Thyroid Hormone ◽  
Trichloroacetic Acid ◽  
Specific Activity ◽  
Acid Precipitation ◽  
Solvent System ◽  
Blood Stream ◽  
Radioactive Materials ◽  
Isotope Technique ◽  
Double Isotope

ABSTRACT The process of secretion of the thyroid hormone involves several steps: pinocytosis of thyroglobulin, fusion of the colloid droplets with the lysosomes, digestion of thyroglobulin by a cathepsin, dehalogenation of tyrosines and release of thyronines into the blood stream. The present paper describes a double isotope technique for studying the first two steps. Thyrotrophin (TSH) administration to rats increased the radioactivity present in all fractions, specially in the 15 000 × g pellet. When the subcellular distribution of acid phosphatase was determined, the highest specific activity was found in this fraction, thus indicating the presence of lysosomes. The content of radioactive materials in the 15 000 × g pellet was analyzed by trichloroacetic acid precipitation and by ascending paper chromatography using n-butanol:ethanol:ammonium hydroxide (5:1:2;v/v) as solvent system. The results obtained showed that 90% of the radioactivity was protein bound and strongly suggest that this material is thyroglobulin.

scholarly journals Does high-mobility-group non-histone protein HMG 1 interact specifically with histone H1 subfractions?

1979 ◽  
Vol 183 (3) ◽  
pp. 657-662 ◽  
Author(s):  
P D Cary ◽  
K V Shooter ◽  
G H Goodwin ◽  
E W Johns ◽  
J Y Olayemi ◽  
...  
Keyword(s):  
Specific Interaction ◽  
High Mobility ◽  
Histone H1 ◽  
High Mobility Group ◽  
Chromosomal Protein ◽  
Histone Protein ◽  
Total Histone ◽  
Equilibrium Sedimentation ◽  
Histone H5

The interaction of the non-histone chromosomal protein HMG (high-mobility group) 1 with histone H1 subfractions was investigated by equilibrium sedimentation and n.m.r. sectroscopy. In contrast with a previous report [Smerdon & Isenberg (1976) Biochemistry 15, 4242–4247], it was found, by using equilibrium-sedimentation analysis, that protein HMG 1 binds to all three histone H1 subfractions CTL1, CTL2, and CTL3, arguing against there being a specific interaction between protein HMG 1 and only two of the subfractions, CTL1 and CTL2. Raising the ionic strength of the solutions prevents binding of protein HMG 1 to total histone H1 and the three subfractions, suggesting that the binding in vitro is simply a non-specific ionic interaction between acidic regions of the non-histone protein and the basic regions of the histone. Protein HMG 1 binds to histone H5 also, supporting this view. The above conclusions are supported by n.m.r. studies of protein HMG 1/histone H1 subfraction mixtures. When the two proteins were mixed, there was little perturbation of the n.m.r. spectra and there was no evidence for specific interaction of protein HMG 1 with any of the subfractions. It therefore remains an open question as to whether protein HMG 1 and histone H1 are complexed together in chromatin.

scholarly journals Subcellular localization of DNA-binding protein BA by immunofluorescence and immunoelectron microscopy

1979 ◽  
Vol 83 (2) ◽  
pp. 462-463 ◽  
Author(s):  
JJ Catino ◽  
H Busch ◽  
Y Daskal ◽  
LC Yeoman
Keyword(s):  
Immunoelectron Microscopy ◽  
Rat Liver ◽  
Human Lymphocytes ◽  
Chromosomal Protein ◽  
Nonhistone Protein ◽  
Quiescent Cells ◽  
Normal Rat ◽  
Normal Human ◽  
Antigen Localization ◽  
Relationship Of

Nonhistone protein BA has been shown to decrease in amount in the chromatin of growth- stimulated normal rat liver (Yeoman et al. 1975. Cancer Res. 35:1249-1255) and in mitogen-stimulated normal human lymphocytes (Yeoman et al. 1976. Exp. Cell Res. 100:47- 55.). Subsequently, protein BA was purified and was shown to prefer to bind to double- stranded A-T-rich DNAs (Catino et al. 1978. Biochemistry. 17:983-987.). Immunization of rabbits with highly purified protein BA has resulted in the production of a specific antibody. A specific immunoreactivity for chromosomal protein BA has been demonstrated by immunoelectrophoresis and double antibody immunoprecipitation analysis with rabbit anti-BA immunoglobulin and IgG fractions. Light microscope examination of normal rat liver crysections by the indirect immunofluorescence procedure has demonstrated a cytoplasmic as well as a nuclear localization for protein BA with a pronounced perinucleolar fluorescence. Immunoelectron microscopy employing the peroxidase antiperoxidase method of antigen localization has confirmed the immunofluorescence data and has show a heterochromatin localization for protein BA. The relationship of the localization of protein BA to gene control in quiescent cells or to configurations of heterochromatin as well as the marked reduction in the amounts of protein BA which occur in stimulated growth states remains to be defined.

scholarly journals Nonhistone protein antigen profiles of five leukemic cell lines reflect the extent of myeloid differentiation

Blood ◽  
1984 ◽  
Vol 63 (3) ◽  
pp. 701-710 ◽  
Author(s):  
A Goldberger ◽  
G Brewer ◽  
LS Hnilica ◽  
RC Briggs
Keyword(s):  
Cell Lines ◽  
Myeloid Cell ◽  
Leukemic Cell ◽  
Nuclear Extract ◽  
Myeloid Differentiation ◽  
Chromosomal Protein ◽  
Protein Antigens ◽  
Nonhistone Protein ◽  
Leukemic Cell Lines ◽  
Chromatin Proteins

Abstract The human leukemic cell lines, K562, KG-1, and HL-60, and the blast subclones, KG-1a and HL-60 blast, were utilized to relate differences in nonhistone protein antigens to stages of myeloid cell differentiation. Chromatin proteins were separated on SDS- polyacrylamide gels, transferred electrophoretically to nitrocellulose sheets, and visualized by the peroxidase-antiperoxidase method of Sternberger. Screening with antisera raised against total and dehistonized chromatin and a nuclear extract from these cells revealed quantitative as well as qualitative differences between the cell lines. A decrease in antigen content seemed to parallel progressive stages of myeloid cell development. The results indicate that a number of chromosomal protein antigens are lost or modified during differentiation. An antigen(s) of approximately 55,000 molecular weight was found in HL-60 chromatin, but was not present in its less differentiated subclone or in the other lines representative of earlier stage cells. Upon the induction of HL-60 cells to mature to end stages with 4 microM retinoic acid, a significant increase in the mol wt 55,000 activity was seen. This antigen was detected only with antisera against HL-60 total chromatin and granulocyte nuclei, and it was found only in normal mature granulocytes and in the later stage cells of the HL-60 culture. Thus, the antigen appears to be associated with a differentiated myeloid function.

Dismantling of a Nuclear Fuel Fabric - Release of Building Rubble and Site: An Overview

2001 ◽  
Author(s):  
Elisabeth T. Aberl ◽  
Karl-Heinz Lehmann
Keyword(s):  
Nuclear Fuel ◽  
Specific Activity ◽  
Total Activity ◽  
Mean Value ◽  
Salt Mine ◽  
Individual Dose ◽  
Dose Limit ◽  
Uranium Fuel ◽  
Industrial Use ◽  
The Individual

Abstract Uranium fuel rods were produced in the nuclear fuel site. The buildings should be dismantled after decontamination and the site should be released for industrial use. The individual dose to the critical group is limited to an annual value of about 10 μSv. The determined specific activity for remediation of the site was a mean value of 60 mBq/g total activity. For the building rubble and soil primarily two pathways, disposal at a landfill and refill of a disused salt mine, were considered. As a result of the investigations the total activity for the disposal at a landfill had to be limited to about 6,6 GBq. For the refill of the salt mine the estimated individual dose fell below the dose limit in the range of 10 μSv/y.

scholarly journals Analysis of histones from the yeast Saccharomyces carlsbergensis

1979 ◽  
Vol 177 (3) ◽  
pp. 917-923 ◽  
Author(s):  
A Pastink ◽  
T A Berkhout ◽  
W H Mager ◽  
R J Planta
Keyword(s):  
Basic Protein ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Saccharomyces Carlsbergensis ◽  
Histone Proteins ◽  
Chromosomal Proteins ◽  
Complete Set ◽  
Higher Eukaryotes ◽  
Main Components ◽  
Eukaryotic Organisms

Basic chromosomal proteins were isolated from the chromatin of the yeast Saccharomyces carlsbergensis by extraction with H2SO4 and were purified by ion-exchange chromatography. Electrophoresis of the purified fraction on acetic acid/urea gels revealed the presence of four main components. These four proteins were identified as histones H2A, H2B, H3 and H4 on the basis of their amino acid composition, molecular weight and solubility properties, all of which are very similar to the corresponding properties of the various histone proteins from other eukaryotic organisms. A fifth basic protein could be isolated from yeast chromatin by extraction with HClO4. The available evidence indicates this protein to be an H1-type histone. Yeast thus appears to contain a complete set of histone proteins which are strongly homologous to the histones occurring in higher eukaryotes.

scholarly journals THE SYNTHESIS OF ACIDIC CHROMOSOMAL PROTEINS DURING THE CELL CYCLE OF HELA S-3 CELLS

1972 ◽  
Vol 52 (2) ◽  
pp. 308-315 ◽  
Author(s):  
T. W. Borun ◽  
G. S. Stein
Keyword(s):  
Cell Cycle ◽  
Protein Synthesis ◽  
Protein Fraction ◽  
Polyacrylamide Gel ◽  
Nuclear Fraction ◽  
Chromosomal Protein ◽  
Chromosomal Proteins ◽  
Kinetics Of ◽  
Mitotic Cells

The kinetics of acidic residual chromosomal protein synthesis and transport were studied throughout the cell cycle in HeLa S-3 cells synchronized by 2 mM thymidine block and selective detachment of mitotic cells. Pulse labeling the cells with leucine-3H for 2 min and then "chasing" the radioactive proteins for up to 3 hr showed that the amount of protein synthesized, transported, and retained in the acidic residual chromosomal protein fraction is greater immediately after mitosis and later in G1 than in the S or G2 phases of the cell cycle. During S, only 20–25% of the proteins synthesized and transported to the acidic residual chromosomal protein fraction are chased during the first 2 hr after pulse labeling, whereas up to 40% of the material entering the residual nuclear fraction in mitosis, G1, and G2 leaves during a 2 hr chase. Polyacrylamide gel electrophoretic profiles of these proteins, at various times after pulse labeling, reveal that the turnover of individual polypeptides within this fraction has kinetics of synthesis and turnover which are markedly different from one another and undergo stage-specific changes.

Radiation Situation at the Tailing Dump of the Stepnogorsk Mining-Chemical Combine and Adjacent Territories. Message I

2018 ◽  
Vol 63 (1) ◽  
pp. 40-47 ◽  
Author(s):  
П. Казымбет ◽  
P. Kazymbet ◽  
М. Бахтин ◽  
M. Bahtin ◽  
Е. Кашкинбаев ◽  
...  
Keyword(s):  
Gamma Radiation ◽  
Specific Activity ◽  
Negative Impact ◽  
Road Construction ◽  
Field Work ◽  
Research Field ◽  
Effective Radiation Dose ◽  
Tailing Dump ◽  
Local Areas ◽  
The Individual

Purpose: Assessment of the radiation situation at the tailing dump of the Stepnogorsk Mining-Chemical Combine (SMCC) and the settlements around. Material and methods: The tailing dumps of the SMCC and the settlements near located of Aksu, Kvartsytka and Zavodskaya were objects of the radioecological research. Field expedition studies were performed during the summer period and consisted in carrying out a detailed gamma survey of the territory of the investigated objects and settlements, sampling of surface waters, vegetation, surface and layered soil samples. In settlements, along with sampling and studying the gamma background, the equivalent equilibrium volume activity of radon daughters in residential and industrial premises was determined. To determine the concentrations of the studied radionuclides a background was selected, within which the levels of their global deposition were studied. To calculate the individual effective radiation dose of the population the National Radiation Protection Board methodology was used as the basis. Results: In the northern part of the tailing dump of the SMCC in the adjoining territory, a radioactive contamination site was found where the specific activity values for 226Ra, 232Th and 210Pb reach values of 1500–2000 Bq/kg. On the territory of the Aksu settlement, 5 local areas with the area from 25 to 1000 m2 were found, with the intensity of ambient dose equivalent of gamma radiation from 0.39 to 0.86 µSv/h. In the Zavodskaya village, two areas with increased levels of gamma radiation intensity were identified. Conclusion: The obtained results of field work and laboratory analytical studies testify to the negative impact of the tailing dump of the SMCC on the environment of adjacent territories, expressed in contamination of soil, water and vegetation with radionuclides. The nature of the abnormal areas on the territory of the settlements of Aksu and Zavodskaya excludes their origin from the tailing dump of the SMCC. The appearance of these areas of contamination may be due to the use of materials of the 3rd class in sanitary and hygienic standards for improvement and road construction. The probable annual effective dose for the population living in the radioactive local areas of the Aksu ~6.5 mSv/year, at the normal rate of 1 mSv/year from man-made radiation sources.

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