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פותח על ידי קלירמאש פתרונות בע"מ -
Comparative effects of growth inhibitors on sterol metabolism in the nematode Caenorhabditis elegans
Year:
1984
Authors :
סבובודה, ג'יימס
;
.
Volume :
79
Co-Authors:
Lozano, R., Insect Physiology Laboratory, ARS, USDA, Beltsville, MD 20705, United States
Chitwood, D.J., Department of Botany, University of Maryland, College Park, MD 20742, USA. Telephone: (301) 344-2389
Lusby, W.R., Department of Botany, University of Maryland, College Park, MD 20742, USA. Telephone: (301) 344-2389
Thompson, M.J., Department of Botany, University of Maryland, College Park, MD 20742, USA. Telephone: (301) 344-2389
Svoboda, J.A., Department of Botany, University of Maryland, College Park, MD 20742, USA. Telephone: (301) 344-2389
Patterson, G.W., Insect Physiology Laboratory, ARS, USDA, Beltsville, MD 20705, United States
Facilitators :
From page:
21
To page:
26
(
Total pages:
6
)
Abstract:
1. An analogous series of dimethylalkyl compounds, consisting of four amines, an amide, and a phosphonate ester, inhibited motility and reproduction of the nematode Caenorhabditis elegans. 2. Dimethylamines with straight-chain lengths of 12, 14, or 16 carbon atoms were equally active nematicides, causing greater than 80% population growth inhibition at a concentration of 25 ppm. 3. The C12 straight-chain amine and its corresponding amide produced similar inhibition and were much more potent than either the corresponding C12 phosphonate or a C12 branched-chain amine. 4. Inhibition of the Δ24-sterol reductase system was exhibited by all four amines, but not by the amide or phosphonate, in the following order of activity: C12 branched-ehain amine > C12 straight-chain amine > C14 amine > C16 amine. 5. The C12 branched amine also blocked the C-24(28)-dehydrogenase system in the conversion of sitosterol to fucosterol, the initial step in sitosterol dealkylation. © 1984.
Note:
Related Files :
animal experiment
Animals
n,n dimethyltetradecylamine
Oxidoreductases
Reproduction
unclassified drug
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/0742-8413(84)90156-7
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
29413
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:46
You may also be interested in
Scientific Publication
Comparative effects of growth inhibitors on sterol metabolism in the nematode Caenorhabditis elegans
79
Lozano, R., Insect Physiology Laboratory, ARS, USDA, Beltsville, MD 20705, United States
Chitwood, D.J., Department of Botany, University of Maryland, College Park, MD 20742, USA. Telephone: (301) 344-2389
Lusby, W.R., Department of Botany, University of Maryland, College Park, MD 20742, USA. Telephone: (301) 344-2389
Thompson, M.J., Department of Botany, University of Maryland, College Park, MD 20742, USA. Telephone: (301) 344-2389
Svoboda, J.A., Department of Botany, University of Maryland, College Park, MD 20742, USA. Telephone: (301) 344-2389
Patterson, G.W., Insect Physiology Laboratory, ARS, USDA, Beltsville, MD 20705, United States
Comparative effects of growth inhibitors on sterol metabolism in the nematode Caenorhabditis elegans
1. An analogous series of dimethylalkyl compounds, consisting of four amines, an amide, and a phosphonate ester, inhibited motility and reproduction of the nematode Caenorhabditis elegans. 2. Dimethylamines with straight-chain lengths of 12, 14, or 16 carbon atoms were equally active nematicides, causing greater than 80% population growth inhibition at a concentration of 25 ppm. 3. The C12 straight-chain amine and its corresponding amide produced similar inhibition and were much more potent than either the corresponding C12 phosphonate or a C12 branched-chain amine. 4. Inhibition of the Δ24-sterol reductase system was exhibited by all four amines, but not by the amide or phosphonate, in the following order of activity: C12 branched-ehain amine > C12 straight-chain amine > C14 amine > C16 amine. 5. The C12 branched amine also blocked the C-24(28)-dehydrogenase system in the conversion of sitosterol to fucosterol, the initial step in sitosterol dealkylation. © 1984.
Scientific Publication
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