RESUMEN
The time-course of the antiexudative effect of the antihistaminic drugs diphenhydramine, phencarol and suprastin was studied in experimental dextran edema of the rat hind limb after intragastric administration of the drugs in a dose of 50 mg/kg. The data obtained were correlated to the time-course of the blood serum drug concentration measured by high pressure liquid chromatography. The relationship between the pharmacological action of the drugs and the mean maintenance dose was depicted by means of computer. It has been shown that the antiexudative activity of diphenhydramine and phencarol is approximately identical, whereas the efficacy of suprastin is several times less.
Asunto(s)
Edema/tratamiento farmacológico , Antagonistas de los Receptores Histamínicos H1/uso terapéutico , Animales , Compuestos de Bencidrilo/sangre , Compuestos de Bencidrilo/uso terapéutico , Cromatografía Liquida , Difenhidramina/sangre , Difenhidramina/uso terapéutico , Evaluación Preclínica de Medicamentos , Edema/sangre , Etilenodiaminas/sangre , Etilenodiaminas/uso terapéutico , Antagonistas de los Receptores Histamínicos H1/sangre , Masculino , Modelos Biológicos , RatasAsunto(s)
Corticoesteroides/metabolismo , Desoxicorticosterona/antagonistas & inhibidores , Litio/farmacología , Natriuresis/efectos de los fármacos , Potasio/orina , Adrenalectomía , Animales , Carbonatos/farmacología , Permeabilidad de la Membrana Celular/efectos de los fármacos , Túbulos Renales/efectos de los fármacos , Masculino , RatasRESUMEN
Mitochondrial monoamine oxidase isolated from bovine brain stem and purified to electrophoretic homogeneity contained 15 SH groups per mole (100000) of protein. The enzyme deaminated tyramine, p-nitro-beta-phenylethylamine, dopamine, 5-hydroxytryptamine, tryptamine but did not deaminate histamine, GABA or spermidine. Oxidation of 9-II SH groups in the MAO by air oxygen was accompanied by appearance of the properties to deaminate histamine or GABA. This qualitative alteration (transformation) in catalytic properties of the enzyme was readily reversed by treatment with reducing agents (dithiothreitol or GSH). No structural alterations detectable by electrophoresis in polyacrylamide gel were observed in course of the qualitative reversible modifications in catalytic activity of MAO. The qualitative alterations in substrate specificity were also initiated by treatment with H2O2 of the monoamine oxidases tightly bound with membrane structures of mitochondria from bovine brain stem.