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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The interaction between bovine serum albumin and dodecahydrododecaborate B_<12>H_<12>^<2-> or mercaptoundecahydrododecaborate B_<12>H_<11>SH^<2-> anion has been investigated by equilibrium dialysis, equilibrium distribution in and out of a Sephadex gel, gel-filtration-, ion-exchange-, and ion-retardation-chromatographies. The results have been discussed with the following conclusions. 1) Both borates are strongly bound to the albumin through ion-pair formation with cationic sites on the protein molecules. 2) This binding of ionic character can be readily broken up by ion-exchange or ion-retardation chromatography. 3) The latter borate shows, in addition, another mode of binding which is resistant against ion-exchange and ion-retardation resins. 4) This binding of covalent character is due to the formation of disulfide linkage between the boron cage of B_<12>H_<11>SH^<2-> and the albumin.
- 公益社団法人日本薬学会の論文
- 1976-12-25
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