Unconjugated bilirubin effect on 3H-ouabain binding to human fetal red cells.
Human fetal red cells show heterogeneity of 3H-ouabain binding sites. These cells were chosen as a model to look into unconjugated bilirubin effects on the primary active Na(+)-K+ transport mechanism. Evidences are presented suggesting that unconjugated bilirubin affects 3H-ouabain binding but not through a direct effect. This is supported by the fact that the "low affinity" subgroup sites of the last mentioned ligand persists after unconjugated bilirubin treatment of cells, whereas the "high-affinity" subgroup disappears.
Corchs
J L
JL
Cátedra de Fisiología Humana, Facultad de Ciencias Médicas, Universidad Nacional de Rosario, Argentina.
Corchs
M J
MJ
Serrani
R E
RE
D001663:Bilirubin / Q000494:pharmacology*; D001665:Binding Sites; D004910:Erythrocyte Membrane / Q000187:drug effects / Q000378:metabolism; D004912:Erythrocytes / Q000187:drug effects*; D005312:Fetal Blood / Q000166:cytology*; D006801:Humans; D008024:Ligands; D010042:Ouabain / Q000378:metabolism*; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors / Q000097:blood*
D008024:Ligands; D010042:Ouabain; D000254:Sodium-Potassium-Exchanging ATPase; D001663:Bilirubin