作者: Cesare Indiveri , Annamaria Tonazzi , Ferdinando Palmieri
DOI: 10.1016/0005-2736(94)90281-X
关键词:
摘要: The transport mechanism of the reconstituted carnitine carrier purified from rat liver mitochondria was investigated kinetically. half-saturation constant (Km) for on internal side liposomal membrane (8.7 mM) found to be much higher than that determined external surface (0.45 mM). exclusive presence a single affinity each indicated unidirectional insertion into proteoliposomes, most probably right-side-out with respect mitochondria. Under these defined conditions bisubstrate initial velocity studies homologous (carnitine/carnitine) and heterologous (carnitine/acylcarnitine) antiport were performed by varying both substrate concentrations. kinetic patterns obtained showed ratio Km/Vmax is not influenced second (non-varied) substrate, which indicates ping-pong mechanism. thus differs all other mitochondrial carriers analyzed so far in state, common sequential type reaction has been found.