Plasma membrane fractions from normal, regenerating liver and the AS-30D
ascites hepatocarcinoma exhibited a high degree of enrichment when a set of plasma membrane
enzyme markers were studied in comparison to the ones associated to the mitochondrial and cytosolic compartments. While the (Ca2+,
Mg2+)-ATPase observed for the plasma membrane fraction isolated from normal liver showed an activity of 1.2 mumoles/mg/min, the regenerating liver and the AS-30D plasma membrane fractions presented a much lower
ATPase activity (0.3 and 0.22 mumoles/mg/min respectively). Despite the differences in
ATPase activity observed between models, the plasma membrane fraction from the AS-30D hepatocarcinoma presented a
calcium transport activity similar to the value observed for the normal system (5.9 and 5.5 nmoles Ca2+/mg/10 min, respectively). Interestingly, the
ATP in equilibrium with Pi exchange experiments carried out with the different plasma membrane fractions revealed that the (Ca2+,
Mg2+)-ATPase contained in the plasma membrane from the AS-30D cells shows an exchange activity of 26 nmoles
ATP in equilibrium with Pi/mg/min, similar to the one observed fo the
enzyme from normal liver (30 nmoles
ATP in equilibrium with Pi/mg/min). Our results suggest that the plasma membrane from the transformed model presents a more efficient mechanism to regulate the movement of
calcium through the
calcium pump, with an optimum expenditure of energy.