Partial characterization of the 1-anilino-8-naphthalene sulfonate-adrenochrome semicarbazide interaction site in erythrocyte ghost membrane fragments.
The effect of adrenochrome semicarbazide on the conformation of erythrocyte ghost membranes has been studied by ANS fluorescence, lipid and sulfhydryl spin labels and circular dichroism. No large conformational alterations in the membrane were detected by these techniques. Noncompetitive quenching of ANS fluorescence by ADCS suggests ADCS to interact with the membrane at sites close to the ANS binding domain.
D000323:Adrenochrome / Q000097:blood*; D000817:Anilino Naphthalenesulfonates / Q000097:blood*; D001665:Binding Sites; D001798:Blood Proteins; D002462:Cell Membrane / Q000648:ultrastructure*; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D004912:Erythrocytes / Q000648:ultrastructure*; D005453:Fluorescence; D006801:Humans; D008433:Mathematics; D010447:Peptide Hydrolases; D010740:Phospholipases; D011485:Protein Binding; D011487:Protein Conformation; D011955:Receptors, Drug; D012663:Semicarbazides / Q000097:blood*; D013816:Thermodynamics
D000817:Anilino Naphthalenesulfonates; D001798:Blood Proteins; D011955:Receptors, Drug; D012663:Semicarbazides; D000323:Adrenochrome; D010740:Phospholipases; D010447:Peptide Hydrolases