Interaction between serum albumin and mercaptoundecahydrododecaborate ion (an agent for boron-neutron capture therapy of brain tumor). I. Introductory remarks and preliminary experiments.

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Abstract
The interaction between bovine serum albumin and dodecahydrododecaborate B12H122- or mercaptoundecahydrododecaborate B12H11SH2- anion was investigated by equilibrium dialysis, equilibrium distribution in and out of a Sephadex gel, gel-filtration-, ion-exchange and ion-retardation-chromatographies. Both borates are strongly bound to the albumin through ion-pair formation with cationic sites on the protein molecules. This binding of ionic character can be readily broken up by ion-exchange or ion-retardation chromatography. The latter borate shows another mode of binding which is resistant against ion-exchange and ion-retardation resins. This binding of covalent character is due to the formation of disulfide linkage between the boron cage of B12H11SH2- and the albumin.

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