RESUMEN

The fluorescence of tryptophan residues in Ca2+--Mg2+-ATPase was studied in the presence of K2PtCl4, K2PdCl4 and 5-sulpho-8-mercaptochinolinate platinum and palladium. It has been shown that both first two compounds quenched the fluorescence dye to bonding with SH-groups in ATPase active centre, but the last two compounds influence the fluorescence by bonding with tryptophan residues. The distance between the SH-groups and tryptophan in the active centre was determined by Foerster--Galanin equation and was equal to 14 +/- 3 A.

Asunto(s)

ATPasas Transportadoras de Calcio/metabolismo , Paladio/farmacología , Platino (Metal)/farmacología , Retículo Sarcoplasmático/enzimología , Animales , Sitios de Unión , ATPasa de Ca(2+) y Mg(2+) , Cinética , Unión Proteica , Conformación Proteica , Conejos , Espectrometría de Fluorescencia , Espectrofotometría/métodos