Asunto(s)
Aminoquinolinas , Inhibidores de la Colinesterasa/farmacología , Membranas Intracelulares/efectos de los fármacos , Fármacos Neuroprotectores/farmacología , Retículo Sarcoplasmático/efectos de los fármacos , Membranas Sinápticas/efectos de los fármacos , Animales , ATPasa de Ca(2+) y Mg(2+)/metabolismo , Espectroscopía de Resonancia por Spin del Electrón , Membranas Intracelulares/enzimología , Piracetam/farmacología , Ratas , Retículo Sarcoplasmático/enzimología , Membranas Sinápticas/enzimología , Tacrina/farmacologíaRESUMEN
The possible use of EPR spectroscopy (spin labelling) for the study of horse liver alcohol dehydrogenase with a silochrome adsorbent is discussed. The rotatory diffusion of nitroxyl labels chemically linked to the enzyme was studied with reference to the time of the enzyme incubation with the adsorbent and the degree of its accumulation on the adsorbent surface. The mobility of nitroxyl radicals attached to the protein globules was shown to increase with time. It was concluded that the conformation of the enzyme molecules changes during their interaction with the adsorbent.
Asunto(s)
Oxidorreductasas de Alcohol/metabolismo , Enzimas Inmovilizadas/metabolismo , Alcohol Deshidrogenasa , Animales , Espectroscopía de Resonancia por Spin del Electrón/métodos , Geles , Caballos , Cinética , Hígado/enzimología , Conformación Proteica , Gel de Sílice , Dióxido de SilicioRESUMEN
Interaction of 8 penicillin preparations with human serum albumin was studied with the spin-labels method and a probe. Correlation between the binding level of penicillins with human serum albumin and their effect on the spectrum of EPR of the spin-label attached to albumin was observed only with the use of a hydrophobic probe (radical III). The covalent attached marks and the hydrophobic probe may be used for rapid orienting estimation of pencillin interaction with albumin.