scholarly journals The Effects of ZnO Nanoparticles in Combination with Alcohol on Biosynthetic Potential of Saccharomyces cerevisiae

2017 ◽  
Vol 21 (2) ◽  
pp. 19-24
Author(s):  
Natalia Chiseliţa ◽  
Agafia Usatii ◽  
Nadejda Efremova
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Synthesis ◽  
Enzyme Activity ◽  
Biomass Production ◽  
Zno Nanoparticles ◽  
Yeast Strain ◽  
Culture Medium ◽  
Inhibit Protein Synthesis ◽  
Maximum Value ◽  
Directed Synthesis

Abstract This paper reports about experimental results concerning the influence of 30 nm ZnO nanoparticles on biomass, carbohydrates, β-glucans, proteins accumulation and catalase enzyme activity at Saccharomyces cerevisiae CNMN-Y-20 yeast strain exposed to alcohol action. Alcohol in concentrations of 2%, 5% and 10% added to culture medium has been reported to stimulate β-glucans biosynthesis and to inhibit protein synthesis. Low biomass production, with 71% less that control, was detected in the experiments with 10% alcohol. ZnO nanoparticles in combination with alcohol do not offer sufficient protection for the proteins biosynthesis, but efficiently protect the carbohydrates and β-glucans biosynthetic processes, which contents in the biomass are with 16.6% and 19.9% higher than control, respectively. The maximum value of β-glucans content was established in case of cultivation of selected yeast strain on YPD medium supplemented with 5 mg/L nanoparticles ZnO and 2% alcohol. The obtained results allowed the elaboration of new procedure for directed synthesis of β-glucans that contributed to an increase of this component with 30.7%, compared to control.

scholarly journals SUPPRESSION OF DELAYED HYPERSENSITIVITY IN VITRO BY INHIBITION OF PROTEIN SYNTHESIS

1965 ◽  
Vol 122 (6) ◽  
pp. 1125-1134 ◽  
Author(s):  
John R. David
Keyword(s):  
Protein Synthesis ◽  
Culture Medium ◽  
Specific Antigen ◽  
Delayed Hypersensitivity ◽  
Cell Protein ◽  
Sensitive Cell ◽  
Active Protein ◽  
Inhibit Protein Synthesis ◽  
Inhibition Of Protein Synthesis

Peritoneal cells from guinea pigs exhibiting delayed hypersensitivity are inhibited from migrating in vitro by specific antigen. This inhibition is prevented by the addition of puromycin to the culture medium. The amount of puromycin necessary to prevent the inhibition by antigen also suppressed the incorporation of C14-leucine into peritoneal cell protein. Additional evidence that the action of puromycin is due to its inhibition of protein synthesis has been obtained with analogues of puromycin; those that inhibit protein synthesis also prevent the action of antigen on the cells, while those analogues that do not inhibit protein synthesis have no effect. Actinomycin also prevents the inhibition of sensitive cells by antigen while chloramphenicol has no effect. The data indicate that the inhibition of sensitive cell migration by antigen requires active protein synthesis. The possible mechanisms by which inhibition of protein synthesis may influence the in vitro reactions of delayed hypersensitivity are discussed.

scholarly journals The evaluation of nanoparticles ZnO and TiO2 effects on Saccharomyces cerevisiae CNMN-Y-20 yeast strain

2016 ◽  
Vol 20 (1) ◽  
pp. 85-92 ◽  
Author(s):  
Agafia Usatîi ◽  
Natalia Chiseliţa ◽  
Nadejda Efremova
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Proliferation ◽  
Yeast Cell ◽  
Protein Content ◽  
Biomass Production ◽  
Yeast Strain ◽  
Cell Membranes ◽  
Carbohydrate Content

Abstract This paper investigates the action of nanoparticles ZnO (10 nm) and TiO2 (30 nm) on growth of Saccharomyces cerevisiae CNMN-Y-20 yeast. Nanoparticles in concentration of 0,5; 1,0 and 5,0 mg/L in YPD medium did not modify significantly cell proliferation, biomass production, the carbohydrate content and the content of β-glucans at Saccharomyces cerevisiae CNMN-Y-20. Nanoparticles ZnO and TiO2 contributed to the decrease in protein content, which demonstrated the appearance of the alterations of yeast cell membranes.

Stability of induced α-glucosidase activity in the absence of inducer

1969 ◽  
Vol 47 (7) ◽  
pp. 677-684 ◽  
Author(s):  
Robert G. Bell
Keyword(s):  
Protein Synthesis ◽  
Enzyme Activity ◽  
Energy Production ◽  
Yeast Cells ◽  
Glucose Medium ◽  
Inhibit Protein Synthesis ◽  
Original Activity ◽  
Glucosidase Activity ◽  
Initial Rise ◽  
Purine Pyrimidine

Yeast cells containing induced α-glucosidase activity lose 10% of the original activity per hour when placed in phosphate buffer – glucose medium. The presence of inducer has no effect on the rate of loss. Induced cells placed in complex medium plus glucose or glycerol show an initial rise in α-glucosidase activity, and then a slow decrease which is accelerated when growth stops. The loss of induced enzyme activity in buffer–glucose medium is inhibited by inhibitors of energy production or protein synthesis whether they are added immediately or 2 or 4 h after suspension of cells in the medium. The ability of the inhibitors to block the loss of induced enzyme activity is correlated with their ability to inhibit protein synthesis. Ammonium sulfate inhibits the loss of α-glucosidase activity after a lag but amino acid or purine–pyrimidine mixtures do not. The loss of induced enzyme activity in cell-free supernatant solutions is less than 2% of the original activity per hour at 30°.

Shedding of cytoplasmic actins by developing muscle cells

1988 ◽  
Vol 89 (2) ◽  
pp. 273-282
Author(s):  
G.M. Denning ◽  
I.S. Kim ◽  
A.B. Fulton
Keyword(s):  
Protein Synthesis ◽  
Electron Microscope ◽  
Culture Medium ◽  
Muscle Cells ◽  
Cytoskeletal Proteins ◽  
Inhibit Protein Synthesis ◽  
Culture Dish ◽  
Cytoplasmic Actin ◽  
Alpha Actin ◽  
Developing Muscle

Young myotubes develop spots or macules of actin and alpha actinin under and adjacent to slender actin strands. Macules are found only before sarcomere formation. They contain cytoplasmic actin, small amounts of alpha actin, and alpha actinin but are devoid of tubulin, myosin and vimentin. In the electron microscope, they are seen to contain small filaments but no other organelles. Macules are found on the culture dish and in the culture medium, as well as on the lower and lateral surfaces of the cells. Both emetine and cycloheximide, at doses that inhibit protein synthesis, accelerate formation and shedding of macules. This presents the first observation of a cellular system in which the changeover from a generalized cytoskeleton to a tissue-specific cytoskeleton involves shedding of the cytoplasmic isoforms of cytoskeletal proteins.

INHIBITION OF THYROGLOBULIN BIOSYNTHESIS AND DEGRADATION BY EXCESS IODIDE. SYNERGISM WITH LITHIUM

1976 ◽  
Vol 81 (2) ◽  
pp. 495-506 ◽  
Author(s):  
A. Radvila ◽  
R. Roost ◽  
H. Bürgi ◽  
H. Kohler ◽  
H. Studer
Keyword(s):  
Protein Synthesis ◽  
Thyroid Gland ◽  
Inhibitory Action ◽  
Inhibit Protein Synthesis ◽  
Thyrotrophic Hormone ◽  
Thyroid Glands ◽  
Pre Treatment ◽  
Excess Iodide ◽  
Kidney Liver

ABSTRACT Lithium and excess iodide inhibit the release of thyroid hormone from preformed stores. We thus tested the hypothesis that this was due to an inhibition of thyroglobulin breakdown. Rats were pre-treated with propylthiouracil (PTU) for 3 weeks in order to deplete their thyroids of thyroglobulin. While the PTU was continued, lithium chloride (0.25 mEq./100 g weight) or potassium iodide (3 mg per rat) were injected every 12 h for 3 days. Thereafter the thyroglobulin content in thyroid gland homogenates was measured. PTU pre-treatment lowered the thyroglobulin content from 4.21 to 0.22 mg/100 mg gland. Lithium caused a marked re-accumulation of thyroglobulin to 0.60 mg/100 mg within 3 days. While iodide alone had only a borderline effect, it markedly potentiated the action of lithium and a combination of the two drugs increased the thyroglobulin content to 1.04 mg/100 mg. Thyroxine was injected into similarly pre-treated animals to suppress secretion of thyrotrophic hormone. This markedly inhibited the proteolysis of thyroglobulin and 1.3 mg/100 mg gland accumulated after 3 days. Excess iodide, given in addition to thyroxine, decreased the amount of thyroglobulin accumulated to 0.75 mg/100 mg gland. To study whether this could be explained by an inhibitory action of iodide on thyroglobulin biosynthesis, thyroid glands from animals treated with excess iodide were incubated in vitro in the presence of 0.2 mm iodide for 3 h. Iodide decreased the incorporation of radioactive leucine into total thyroidal protein and into thyroglobulin by 25 and 35 % respectively. Iodide did not inhibit protein synthesis in the kidney, liver or muscle tissue. Thus, large doses of iodide selectively inhibit thyroglobulin biosynthesis.

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