Studies on the binding of 1-anilino-8-naphthalene sulfonate to very low density and high density himan serum lipoproteins.
Very low density and high density lipoproteins have been isolated from human plasma and their interaction with 1-anilin0-8-naphthalene sulfonate has been studied under different conditions of pH and added salt. Intrinsic fluorescence of bound 1-anilino-8-naphthalene sulfonate was higher for high density lipoproteins then for very low density lipoproteins, but was unaffected by salt in both systems. Binding of 1-anilino-8-naphthalene sulfonate by both these lipoproteins was saturable and was higher in the presence of added NaCl or CaCl2, Ca2+ having a greater effect than Na+ in enhancing fluorescence. The binding data were analyzed by Scatchard plots; the number of binding sites and the affinity of 1-anilino-8-naphthalene sulfonate for the site increased with increasing salt concentration. Fluorescence pH curves were similar to those published for phospholipids. From these and previous observations it is suggested that the phospholipids probably represent the major binding sites for 1-anilino-8-naphthalene sulfonate.
D000817:Anilino Naphthalenesulfonates; D001059:Apoproteins / Q000097:blood; D001665:Binding Sites; D002122:Calcium Chloride; D002784:Cholesterol / Q000032:analysis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008075:Lipoproteins, HDL / Q000097:blood; D008079:Lipoproteins, VLDL / Q000097:blood; D009994:Osmolar Concentration; D010743:Phospholipids / Q000032:analysis; D011485:Protein Binding; D011487:Protein Conformation; D012965:Sodium Chloride; D013050:Spectrometry, Fluorescence
D000817:Anilino Naphthalenesulfonates; D001059:Apoproteins; D008075:Lipoproteins, HDL; D008079:Lipoproteins, VLDL; D010743:Phospholipids; D012965:Sodium Chloride; D002784:Cholesterol; D002122:Calcium Chloride