The B°AT1 amino acid transporter from rat kidney reconstituted in liposomes: Kinetics and inactivation by methylmercury

B°AT1 transporter reconstituted in liposomes does not require collectrin for function. ► The transporter catalyses Gln-Na+ cotransport by random simultaneous mechanism. ► Methylmercury inactivates the transporter; N-acetylcysteine reverses this effect. ► A CXXC motif of B°AT1 close to the membrane is a possible binding site of mercurials.