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3.
J Pharmacol Exp Ther ; 209(2): 215-8, 1979 May.
Artigo em Inglês | MEDLINE | ID: mdl-438996

RESUMO

In vivo hepatic protein synthesis was monitored in female rats under control and smoke-exposed conditions. During the 15 min period after i.v. administration of [3H]proline protein synthesis was 206 +/- 35 nmol of proline per mg of DNA for sham-control animals. When animals were subjected to acute exposure to cigarette smoke, protein synthesis was inhibited and the extent of inhibition was positively correlated with the dosage of smoke (32%, 15 puffs; 66%, 60 puffs). The inhibitory effect of whole smoke on protein synthesis was unaltered by passing the smoke through either charcoal or cambridge filters. Carbon monoxide in smoke is not removed by either type of filter. At a level comparable to that in cigarette smoke carbon monoxide depressed hepatic protein synthesis to the same extent as did whole or filtered smoke.


Assuntos
Fígado/metabolismo , Biossíntese de Proteínas , Fumar/metabolismo , Animais , Monóxido de Carbono/farmacologia , Carboxihemoglobina/metabolismo , DNA/metabolismo , Feminino , Filtração , Fígado/efeitos dos fármacos , Prolina/metabolismo , Ratos
4.
J Pharm Sci ; 68(3): 377-8, 1979 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-423135

RESUMO

Twelve 1-phenyl-2-(phenylcarbamoyl)pyrazolidines were synthesized from 1-arylpyrazolidines and aryl isocyanates. These adducts showed little anticonvulsant activity in the maximal electroshock seizure and pentylenetetrazol seizure assays.


Assuntos
Anticonvulsivantes/síntese química , Pirazóis/síntese química , Animais , Eletrochoque , Camundongos , Pentilenotetrazol/antagonistas & inibidores , Pirazóis/farmacologia , Relação Estrutura-Atividade
5.
Environ Res ; 17(2): 205-15, 1978 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-318514

RESUMO

The present investigation was conducted to determine the rate of collagen and non-collagen protein synthesis by rat lung under in vitro conditions. The rate of synthesis of non-collagen protein was greater than the rate of collagen synthesis in animals between 1 and 95 days of age. Synthesis of both types of proteins was highest in 1-day-old animals. Rate of synthesis of non-collagen protein was markedly diminished after 7 days of age and that of collagen decreased after 14 days. Per gram lung, the total amount of collagen increased 3.5-fold between Day 7 and 95 whereas total protein was relatively constant. When lung was exposed to smoke under in vitro conditions synthesis of collagen and non-collagen protein was almost completely depressed.


Assuntos
Colágeno/biossíntese , Exposição Ambiental , Pulmão/crescimento & desenvolvimento , Fumar/efeitos adversos , Fatores Etários , Animais , Colágeno/antagonistas & inibidores , DNA/análise , Humanos , Kentucky , Cinética , Ratos , Ratos Endogâmicos
7.
J Pharm Sci ; 66(1): 111-3, 1977 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-833724

RESUMO

Aqueous suspensions of aspirin or acetaminophen (125 and 250 mg/kg/day) were administered orally to pregnant Sprague-Dawley rats on Days 8-19 of gestation Day 20, each rat was sacrificed and the uterus was examined in situ. Each fetal-placental unit was resected and examined. Fetuses from rats given 125 or 250 mg/kg/day of aspirin were shorter and weighed less than those obtained from control rats. In animals receiving the higher dose of aspirin, the placentas were smaller and the number of fetal resorptions was increased. Acetaminophen (250 mg/kg/day) did not affect fetal length or weight or the incidence of resorption. Acetaminophen interfered less with the normal growth of the rat fetus and placenta than did aspirin.


Assuntos
Acetaminofen/farmacologia , Aspirina/farmacologia , Feto/efeitos dos fármacos , Placenta/efeitos dos fármacos , Animais , Peso Corporal/efeitos dos fármacos , Feminino , Gravidez , Ratos
8.
J Cell Physiol ; 87(1): 63-9, 1976 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-173725

RESUMO

Incubation of rabbit erythrocytes with 32Pi resulted in labeling of membrane diphosphoinositide, triphosphoinositide, and phosphatidic acid. Hypotonic lysis at 37 degress C resulted in an extremely rapid breakdown of the labeled polyphosphoinositides. This breakdown could be retarded by lysis in the presence of EDTA and by lowering the temperature to 0 degrees thus allowing preparation of membranes with minimum breakdown of the labeled lipids. Rapid breakdown of di- and triphosphoinositide in isolated membranes could be initiated by Ca++ or to a lesser extent by Mg++ and prevented by detergents and by heating to 75 degrees C. Assay of radiolabeled lipid was carried out by a method which bypassed prior lipid extraction and which enabled sequential sampling of reactions at 10-second intervals. This method was more convenient than standard procedures and gave yields of di- and triphosphoinositide equivalent to that obtained by the method of Folch.


Assuntos
Eritrócitos/metabolismo , Fosfatidilinositóis/metabolismo , Animais , Cálcio/farmacologia , Membrana Celular/metabolismo , Ácido Edético/farmacologia , Hemólise , Cinética , Magnésio/farmacologia , Ácidos Fosfatídicos/metabolismo , Polissorbatos/farmacologia , Potássio/farmacologia , Coelhos , Sódio/farmacologia , Dodecilsulfato de Sódio/farmacologia
11.
Biochim Biophys Acta ; 382(1): 58-64, 1975 Feb 28.
Artigo em Inglês | MEDLINE | ID: mdl-164238

RESUMO

1. Impermeable inside-out and right-side-out vesicles were prepared from membranes of human erythrocytes. During preparation of each kind of impermeable vesicle, permeable vesicles were also obtained. 2. Incubation of vesicles with [gamma-32P]ATP at 37 degrees C for periods of up to 1 hr did not change the topography or the permeability of the vesicles. 3. Vesicles incorporated labeled phosphate from [gamma-32P]ATP into both diphosphoinositide and triphosphoinositide, but impermeable inside-out vesicles incorporated significantly more nuclide than did right-side-out vesicles. 4. Permeable vesicles derived during the preparation of inside-out vesicles were as active as impermeable inside-out vesicles in the incorporation of labeled phosphate into the polyphosphoinositides. However, permeable vesicles derived during the preparation of right-side out vesicles were not as active. 5. Impermeable right-side-out vesicles, treated with 0.01 percent saponin, incorporated labeled phosphate into the polyphosphoinositides at a level comparable to that of impermeable inside-out vesicles. 6. These data show that the enzymes involved in metabolism of diphosphoinositide and triphosphoinositide are located on the cytoplasmic surface of the erythrocyte membrane.


Assuntos
Eritrócitos/metabolismo , Fosfatidilinositóis/sangue , Acetilcolinesterase/sangue , Trifosfato de Adenosina/metabolismo , Membrana Celular/metabolismo , Permeabilidade da Membrana Celular , Gliceraldeído-3-Fosfato Desidrogenases/sangue , Humanos , Polietilenoglicóis , Fatores de Tempo
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