The interaction of resealed reticulocyte ghosts with Fe3+-transferrin-CO3(2-).
The present studies were designed to investigate the interaction of Fe3+transferrin-CO3(2-) with the transferrin receptors of the resealed reticulocyte ghost and to assess the degree to which the iron release reaction can be reconstituted in resealed ghosts supplemented with entrapped cytoplasmic components. Reticulocyte, but not erythrocyte, ghosts displayed an intact Fe3+transferrin-CO3(2-) binding capability. When ATP, NADH and ferritin were included during the resealing process, some iron release to the ghosts was observed.
Loh
T T
TT
Shupe
K
K
Bates
G W
GW
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D007700:Kinetics; D009243:NAD / Q000378:metabolism; D011817:Rabbits; D011956:Receptors, Cell Surface / Q000378:metabolism; D011990:Receptors, Transferrin; D012156:Reticulocytes / Q000378:metabolism*; D013696:Temperature; D014168:Transferrin / Q000378:metabolism*
D011956:Receptors, Cell Surface; D011990:Receptors, Transferrin; D014168:Transferrin; D009243:NAD; D000255:Adenosine Triphosphate