Steroid-Protein Interactions by Ulrich Westphal (auth.)

By Ulrich Westphal (auth.)

This is the tale of steroid-protein interactions as one investigator sees it. Following the overall proposal of this monograph sequence, it emphasizes the consequences and interpretations acquired within the author's laboratory, and is accordingly a subjective account. spotting, how­ ever, that the dialogue of the topic will be incomplete if the cloth have been constrained to 1 scientist's paintings, the fundamental in achieving­ ments of alternative investigators were included. An attempt has therefore been made to provide a balanced presentation and to allow the reader to determine in standpoint the numerous aspects of the interactions among steroids and proteins. considering that this is often the 1st finished therapy of the subject, it kind of feels applicable to visit the roots, and check out to determine the way it began. the 1st chapters, accordingly, take the reader to the laboratories of these who very early conceived the importance of the attachment of dyes, medications, and different conspicuous molecules to these colloids referred to as proteins. the invention of the steroid hormones set the degree for significant research in their interplay with proteins of varied origins and services - a strategy that is carrying on with at the present time with expanding vigor.

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Allosteric effect of the lipophilic molecules of the organic solvent on the protein structure. Weak competition of toluene or hexanol with protein binding of dye anions has been observed (KARUSH, 1951). Although SCHELLMAN et al. (1954) assume competition effects to be smaller for n-heptane, it is now definitely established that n-alkanes, e. , butane, pentane and others, form association complexes with several pure proteins (WISHNIA, 1962; WISHNIA and PINDER, 1966). Interactions between hydrocarbons and proteins have been studied by MOHAMMADZADEH-K et al.

Basic Methods for Determination of Steroid-Protein Interactions 1963). If to the aqueous phase a protein is added which forms complexes with the solute, the concentration of the unbound solute in the aqueous phase decreases, and solute moves in from the organic phase to compensate for the decrease. If the partition coefficient, which pertains to the unbound solute in the two phases, remains unaffected by the presence of the protein, a determination of the new equilibrium concentration of the solute in the organic solvent allows calculation of the corresponding concentration of unbound ligand in the aqueous protein phase, and thus by difference that of the bound portion.

The similarity to the adsorption isotherm was then the closest approach to a quantitative treatment available. Although some of the methods introduced at the time have later been developed to useful quantitative procedures, others do not lend themselves readily for this purpose. For example, influence on surface tension (LECOMTE DU N OUY, 1922, 1928) is exerted by only a limited number of steroid compounds; this technique has played no further role in the investigation of steroid-protein interaction.

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