Identification of an ATP-dependent copper transport system in endoplasmic reticulum vesicles isolated from rat liver.

1. This paper identifies and characterizes an ATP-dependent copper transport system in endoplasmic reticulum vesicles isolated from male rat liver. 2. The transporter has a Km of 2.5 +/- 1.2 mumol 1(-1) copper glutathione (CuGSH) and a Vmax of 4.5 +/- 1.3 nmol (mg protein)-1 (5 min)-1 for copper. 3. At a copper concentration of 2 mumol l-1, ATP dependence reaches saturation, with a Km for ATP of 4.7 +/- 2.4 mmol l-1 and a Vmax of 2.8 +/- 0.6 nmol (mg protein)-1 (5 min)-1. 4. The uptake is dependent on ATP hydrolysis, since a low energy analogue of ATP, adenosine 5'-[beta-gamma-methylene] triphosphate tetralithium (AMP.PCP), has no effect on copper uptake. 5. The transporter is a P-type ATPase, since vanadate inhibits uptake with a high degree of specificity (100 mumol l-1 inhibits uptake by 50% at a copper concentration of 2 mumol l-1).