RESUMO
The article is devoted to the inventive activity of the Department of Metabolism Regulation of the Palladin Institute of Biochemistry of NAS of Ukraine in the context of the history of its inception, development and the research activities of its founder, academician of NAS of Ukraine M. F. Guly as well as his students and followers. It briefly tells about practical achievements of M. F. Guly which were as significant, immense and diverse as his scientific accomplishments. The paper analyses in detail the practical results of scientific research of his students and followers aimed to solve practical problems of medicine, food-processing, agriculture, and which are essentially a continuation of the ideas and projects of M. F. Guly.
Assuntos
Academias e Institutos/história , Bioquímica/história , Invenções/história , História do Século XX , História do Século XXI , Ucrânia , Recursos HumanosAssuntos
Academias e Institutos/história , Bioquímica/história , Biofarmácia , Biotecnologia , Ciência de Laboratório Médico , Biofarmácia/história , Biofarmácia/métodos , Biotecnologia/história , Biotecnologia/métodos , História do Século XX , História do Século XXI , Ciência de Laboratório Médico/história , Ciência de Laboratório Médico/métodos , UcrâniaRESUMO
Experiments with highly purified preparations of Ca2+,Mg2+-ATPase solubilized from sarcolemma and a fraction of inside-out sarcolemmal vesicles were performed to study the kinetics of inhibitory effects of eosin Y (0-100 microM) on the catalytic and transport activity of Mg2+,ATP-dependent calcium pump of myometrial cell plasma membrane. For both the Ca2+,Mg2+-dependent ATP hydrolysis and the Mg2+, ATP-dependent accumulation of Ca2+ the apparent inhibitory constant Ki was 0.8 microM. However, eosin Y used at concentrations of up to 100 microM had absolutely no effect on Na+-Ca2+ exchange in the plasma membrane fraction. This inhibitor decreased the turnover rate of purified Ca2+,Mg2+-ATPase determined both by Mg2+ and ATP. However, the affinity of purified Ca2+,Mg2+-ATPase for Mg2+ increased, and its affinity for ATP decreased in the presence of eosin Y. In the case of Mg2+,ATP-dependent Ca2+ transport, eosin Y decreased the turnover rate of the calcium pump whose affinity for Mg2+ and ATP displayed virtually no dependence on the presence of the inhibitor in the incubation medium. The possibility of the use of eosin Y in model experiments for identification of Mg2+, ATP-dependent and Na+-dependent calcium fluxes from smooth muscle cells into the intercellular milieu is discussed.
