Aug 16, 1976

The non-convalent binding of small molecules by ligandin. Interactions with steroids and their conjugates, fatty acids, bromosulphophthalein carcinogens, glutathione and realted compounds

European Journal of Biochemistry
E TippingG Enderby


1. Equilibrium dialysis studies have been made of the binding of a number of small molecules by rat ligandin. Direct measurements of binding together with competition experiments indicated that bromosulphophthalein, oestrone sulphate and dehydroepiandrosterone sulphate each bind at the same single primary binding site with association constants of 1.1 X 10(7), 6.6 X 10(5) and 2.6 X 10(5) 1/mol respectively at pH 7.0,IO.16M,4 degrees C. As well as bromosulphophthalein and dehydroepiandrosterone sulphate, a number of strucurally similar organic anions including 2-hydroxyoestradiol-glutathione oestrone glycyronide, N-methyl-4-aminoazobenzene-glutathione and several bile acids, were able to displace oestrone sulphate from ligandin in a manner consistent with competition at a single binding site. From these experiments association constants for the competing ligands were derived; these were inthe range 1 X 10(4)-1 X 10(6) 1/mol. 2. Ligandin was found to bind a number of compounds for which, because of their low aqueous solubilities relative to their binding affinities complete binding isotherms could bot be obtained. These included several steroids (but not cortisol), 20-methylcholanthrene, diethylstilboestrol, oleate and palmitate....Continue Reading

Mentioned in this Paper

Tumor Promoters
Serum Albumin Measurement
Bile Acid Measurement
Estrone Measurement
Structure-Activity Relationship

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