INFLUENCE OF INHIBITORS OF DNA AND PROTEIN SYNTHESIS ON THE KINETICS OF DNA UPTAKE IN NEISSERIA MENINGITIDIS TRANSFORMATION

2009 ◽  
Vol 77 (3) ◽  
pp. 477-488 ◽  
Author(s):  
Kaare Jyssum
Keyword(s):  
Protein Synthesis ◽  
Neisseria Meningitidis ◽  
Dna Uptake ◽  
Dna And Protein Synthesis ◽  
Kinetics Of

Kinetics of Protein Synthesis in Enucleate Frog Oocytes

Science ◽  
1968 ◽  
Vol 160 (3832) ◽  
pp. 1115-1117 ◽  
Author(s):  
R. E. Ecker ◽  
L. D. Smith ◽  
S. Subtelny
Keyword(s):  
Protein Synthesis ◽  
Kinetics Of ◽  
Kinetics Of Protein Synthesis

Cellular DNA and protein synthesis in reovirus-infected L cells

Virology ◽  
1969 ◽  
Vol 39 (2) ◽  
pp. 357-360 ◽  
Author(s):  
William D. Ensminger ◽  
Igor Tamm
Keyword(s):  
Protein Synthesis ◽  
L Cells ◽  
Dna And Protein Synthesis ◽  
Cellular Dna

scholarly journals Identification in skeletal muscle of a distinct extracellular pool of amino acids, and its role in protein synthesis

1971 ◽  
Vol 121 (5) ◽  
pp. 817-827 ◽  
Author(s):  
R. C. Hider ◽  
E. B. Fern ◽  
D. R. London
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Incubation Medium ◽  
Extensor Digitorum Longus ◽  
Extensor Digitorum ◽  
Longus Muscle ◽  
Kinetics Of

1. The kinetics of radioactive labelling of extra- and intra-cellular amino acid pools and protein of the extensor digitorum longus muscle were studied after incubations with radioactive amino acids in vitro. 2. The results indicated that an extracellular pool could be defined, the contents of which were different from those of the incubation medium. 3. It was concluded that amino acids from the extracellular pool, as defined in this study, were incorporated directly into protein.

scholarly journals Decomposition of time-dependent fluorescence signals reveals codon-specific kinetics of protein synthesis

2018 ◽  
Vol 46 (22) ◽  
pp. e130-e130 ◽  
Author(s):  
Nadin Haase ◽  
Wolf Holtkamp ◽  
Reinhard Lipowsky ◽  
Marina Rodnina ◽  
Sophia Rudorf
Keyword(s):  
Protein Synthesis ◽  
Time Dependent ◽  
Kinetics Of ◽  
Kinetics Of Protein Synthesis

Determination of protein replacement rates by deuterated water: validation of underlying assumptions

2007 ◽  
Vol 292 (5) ◽  
pp. E1340-E1347 ◽  
Author(s):  
Emmanuelle Belloto ◽  
Frédérique Diraison ◽  
Alexandra Basset ◽  
Gwenola Allain ◽  
Pauline Abdallah ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Peripheral Circulation ◽  
Deuterated Water ◽  
Deuterium Labeling ◽  
Kinetics Of ◽  
Glycolytic Rate ◽  
Slow Turnover ◽  
Correct Estimate

H2O administration has recently been proposed as a simple and convenient method to measure protein synthesis rates. 2H2O administration results in deuterium labeling of free amino acids such as alanine, and incorporation into proteins of labeled alanine can then be used to measure protein synthesis rates. We examined first whether during 2H2O administration plasma free alanine enrichment is a correct estimate of the enrichment in the tissue amino acid pools used for protein synthesis. We found that, after 2H2O administration, deuterium labeling in plasma free alanine equilibrated rapidly with body water, and stable enrichment values were obtained within 20 min. Importantly, oral administration of 2H2O induced no difference of labeling between portal and peripheral circulation except for the initial 10 min after a loading dose. The kinetics of free alanine labeling were comparable in various tissues (liver, skeletal muscle, heart) and in plasma with identical plateau values. We show next that increased glycolytic rate or absorption of unlabeled amino acids from ingested meals do not modify alanine labeling. Calculated synthesis rates of mixed proteins were much higher (20- to 70-fold) in plasma and liver than in muscle and heart. Last, comparable replacement rates of apoB100-VLDL were obtained in humans by using the kinetics of incorporation into apoB100 of infused labeled leucine or of alanine labeled by 2H2O administration. All of these results support 2H2O as a safe, reliable, useful, and convenient tracer for studies of protein synthesis, including proteins with slow turnover rate.

Effects of albumin-bilirubin complexes with syngeneic or allogeneic albumin on DNA and protein synthesis in liver and spleen of partially hepatectomized rats

1994 ◽  
Vol 21 (6) ◽  
pp. 947-952 ◽  
Author(s):  
Olga Yu Abakumova ◽  
Ludmila M. Fedorova ◽  
Andrey A. Popov ◽  
Vladimir S. Li ◽  
Susanna L. Arkhangelskaya ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Dna And Protein Synthesis

An in vitro bioassay for a mulluscan gonadotropin

1975 ◽  
Vol 62 (2) ◽  
pp. 433-446
Author(s):  
M. J. Wells ◽  
R. K. O'Dor ◽  
S. K. Buckley
Keyword(s):  
Protein Synthesis ◽  
High Rate ◽  
Follicle Cells ◽  
Octopus Vulgaris ◽  
Amino Acid Incorporation ◽  
Gland Extract ◽  
Acid Incorporation ◽  
Kinetics Of

1. Protein synthesis occurs at a high rate in the ovaries of maturing Octopus vulgaris and can be measured from the incorporation of [14C]leucine in vivo and in isolated groups of eggs in vitro. 2. Removal of the optic glands in vivo 1--3 days prior to testing markedly reduces amino acid incorporation in vivo or in vitro. After 5 days in vivo incorporation stops. 3. The rate of incorporation in vitro is increased by the addition of optic gland extract. 4. Analysis of the kinetics of leucine uptake and incorporation in vitro indicates that the hormone has an effect on the inward transport of leucine which is independent of its action on protein synthesis. 5. Electron-microscope studies of the follicle cells and ova show that the former are the site of protein synthesis. 6. Changes in either uptake or incorporation into protein by the follicle cells can be used as a qualitative biolobical assay for the optic gland hormone. Uptake is very easy to measure but incorporation is the more sensitive parameter. Either is potentially suitable as a quantitative assay for this and perhaps also for other molluscan gonadotropins.

scholarly journals ANTAGONISM BY DIBUTYRYL ADENOSINE CYCLIC 3',5'-MONOPHOSPHATE AND TESTOSTERONE OF CELL ROUNDING REACTIONS

1973 ◽  
Vol 59 (2) ◽  
pp. 471-479 ◽  
Author(s):  
Brian Storrie
Keyword(s):  
Growth Rate ◽  
Protein Synthesis ◽  
Cell Growth ◽  
Concanavalin A ◽  
Divalent Cations ◽  
Cell Growth Rate ◽  
Dibutyryl Camp ◽  
Cell Rounding ◽  
Drug Removal ◽  
Kinetics Of

In an attempt to understand further the mechanism of the morphological and functional "reverse transformation" of CHO-K1 cells induced by dibutyryl adenosine cyclic 3',5'-monophosphate (cAMP) and testosterone, the kinetics of variation in the susceptibility of cells to rounding after the addition or deletion of dibutyryl cAMP and testosterone have been investigated. Changes in susceptibility to cell rounding upon removal of divalent cations or pulse exposure to concanavalin A were complete within 0.5–1 h after addition or deletion of drug. In comparison, the gross conversion of CHO-K1 cells from epithelial- to fibroblast-like morphology after drug treatment or the converse change after drug removal required 8 or 4 h, respectively. The effects on cell rounding are not caused by an effect of dibutyryl cAMP upon cell growth rate. Inhibitor experiments indicate that the changes investigated do not require continued RNA or protein synthesis and are not prevented by agents which depolymerize microtubules.

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