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Interaction among bovine serum albumin(BSA), sodium dodecyl sulfate(SDS), and hydroxyapatite(HAP) was studied in a phosphate buffer solution(pH 7.0) containing 0.02 % sodium azide as an antiseptic at 25•Ž. Both BSA and SDS were simultaneously adsorbed on the surface of HAP. Adsorption amount of SDS in its low concentration range was higher in the presence than in the absence of BSA due to the complex formation between them on the surface of HAP. On the contrary, that of BSA decreased and levelled off after attaining a maximum with an increase in a concentration of SDS. The increase in the adsorption amount of BSA is by virtue of the formation of SDS-BSA complex on the surface. The decrease is owing mainly to the expansion/denaturation of BSA molecule through the complex formation with much amount of SDS on the surface of HAP. INTRODUCTION One of the technics for purification/separation of proteins is an HAP chromatography in the presence of SDS in a phosphate buffer solution.1-3 -57Although it is often practically used, its separation mechanism is not yet elucidated thoroughly. This is because the interactions among HAPSDS-proteins-phosphate ions are so complicated. In the present paper, these interactions were studied with a batch method. BSA was taken as a model protein, for it has been well characterized in its adsorption properties to date.4-5 The interactions studied here were those between (A)BSA-SDS, (B)SDS-HAP, (C)HAP-BSA, and (D)BSA-SDS-HAP in a phosphate buffer solution of pH 7.0 (see Fig. 1). (A) COMPLEX FORMATION BETWEEN BSA-SDS Binding ratio of SDS to BSA in an aqueous phase was determined by means of equilibrium dialysis method. The ratio once increased and then decreased with a concentration of free SDS. The decrease was owing to a decrease in thermodynamic activity of dodecyl sulfate anion (DS-) in a concentration range higher than its c.m.c.(critical micellization concentration). The binding ratio, on the contrary, increased with a concentration of phosphate buffer due to its salting-out effect on SDS and to its shielding effect against electrostatic repulsion between DSand FIGURE 1. Interactions among three components in a phophate buffer of pH 7.0.

COMPLEX FORMATION OF BOVINE SERUM ALBUMIN WITH SODIUM DODECYL SULFATE ON THE SURFACE OF HYDROXYAPATITE