RESUMO
Antianginal hypotensive preparations chloracyzin and stenopryl, antiarrhythmic aimalin as well as local anesthetic and antiarrhythmic trimekaine hydrochloride were studied for their effect on the K+ inflow and outflow rate in the rat liver mitochondria during Sr2+-induced vibrations. In spite of differences in the chemical structure and pharmacological effect, all these substances are shown to uniformly suppress ion flow vibrations in mitochondria, inhibiting K+ outflow. It is found that the inhibition of the K+ outflow rate depends on the concentration of the preparations. Activity of the studied substances as to inhibition of K+ outflow from mitochondria correlates with their pharmacologic activity.
Assuntos
Acetanilidas/farmacologia , Ajmalina/farmacologia , Mitocôndrias Hepáticas/efeitos dos fármacos , Fenetilaminas/farmacologia , Fenotiazinas/farmacologia , Potássio/metabolismo , Trimecaína/farmacologia , Animais , Transporte Biológico/efeitos dos fármacos , Depressão Química , Dinitrofenóis/farmacologia , Ratos , Ratos EndogâmicosAssuntos
Oligorribonucleotídeos , Retinose Pigmentar/tratamento farmacológico , Ribonucleotídeos/uso terapêutico , Adulto , Ensaios Clínicos como Assunto , Adaptação à Escuridão/efeitos dos fármacos , Eletrorretinografia , Feminino , Humanos , Ribonucleotídeos/administração & dosagem , Fatores de Tempo , Campos Visuais/efeitos dos fármacosAssuntos
Surdez/diagnóstico , Oligorribonucleotídeos , Retinose Pigmentar/diagnóstico , Adolescente , Adulto , Surdez/tratamento farmacológico , Avaliação de Medicamentos , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Retinose Pigmentar/tratamento farmacológico , Ribonucleotídeos/administração & dosagem , Percepção da Fala/efeitos dos fármacos , Síndrome , Acuidade Visual/efeitos dos fármacosRESUMO
The pH-dependence of the reduction rate of ferricytochrome C by intact and chemically modified oxymyoglobins has been studied. The modification was performed with respect to histidine residues and alpha-aminogroup of N-terminal valine. Two histidine residues of myoglobin, His A10 and His GH1, are shown to take part in the realization of the "active" contact between the molecules in the course of the reaction. The deprotonation of the first residue contributes to the acceleration and that of the second to the reduction of the reaction. The found orientation of the Mb molecules in the "active complex" implies that at any orientation of cytochrome C the distance between the haemes of the both molecules should be more than 30 A. This makes highly probable that a structure-dependent mechanism of electron transfer in the system under study can be proposed.
