title: Studies on the binding characteristics of antimycin A and albumin in relation to the inhibitor activity of the complex on rat proximal tubular sodium transport.
abstract: As reported previously [11] Antimycin A is effective in inhibiting sodium transport of the proximal tubule only when applied to the luminal side and in the presence of albumin. Therefore the interaction of Antimycin A with albumin was examined with the technique of equilibrium dialysis. It was found that Antimycin A was bound to albumin at five sites with a dissociation constant of 2.5 X 10(-6) M. This finding suggests that Antimycin A is taken up by the tubular cell as an Antimycin A/albumin complex via pinocytosis. In the pinocytotic vesicle this complex probably dissociates, and free Antimycin A is released into the cytoplasm where it can reach it's sites of action in the mitochondria and at the plasma membrane. This uptake mechanism might provide a general method to incorporate substances into the cell which do not penetrate the plasma membrane.
mesh_terms: D000968:Antimycin A / Q000378:metabolism* / Q000494:pharmacology; D001692:Biological Transport; D007687:Kidney Tubules, Proximal / Q000187:drug effects / Q000378:metabolism*; D010420:Pentanes / Q000494:pharmacology; D010728:Phosphoenolpyruvate / Q000494:pharmacology; D010873:Pinocytosis; D012709:Serum Albumin / Q000378:metabolism* / Q000494:pharmacology; D012964:Sodium / Q000378:metabolism*
chemical_list: D010420:Pentanes; D012709:Serum Albumin; D000968:Antimycin A; D010728:Phosphoenolpyruvate; D012964:Sodium