Low-Mr iron isolated from guinea pig reticulocytes as AMP-Fe and ATP-Fe complexes.
Guinea pig reticulocytes were pulse-labelled with 59Fe bound to transferrin. Haemolysates prepared from these reticulocytes were subjected to rapid (NH1)2SO1 precipitation and then chromatography on an anion-exchange resin. ATP-bound 59Fe was the dominant species in the reticulocyte cytosol; 2,3-bisphosphoglycerate and GTP iron complexes were not detected despite the fact that these were stable with (NH1)2SO1 precipitation and readily detected with anion-exchange chromatography. AMP-bound Fe was a minor component of the cytosol following rapid (NH1)2SO4 precipitation, and the major component when iron was released from transferrin by haemolysates. We speculate that ATP-Fe may be degraded in the cell to permit utilization of its iron for haem synthesis.
Weaver
J
J
Department of Medicine, Albert Einstein College of Medicine, Bronx, NY 10461.
Pollack
S
S
D000249:Adenosine Monophosphate / Q000097:blood*; D000255:Adenosine Triphosphate / Q000097:blood*; D000818:Animals; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000032:analysis; D006168:Guinea Pigs; D007501:Iron / Q000097:blood*; D008024:Ligands; D008970:Molecular Weight; D012156:Reticulocytes / Q000032:analysis*
D008024:Ligands; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D007501:Iron