The binding of calcium and yttrium ions to a glycoprotein from bovine cortical bone

Abstract

The binding of Ca2+ and Y3+ to an acidic glycoprotein from bovine cortical bone, bone sialoprotein, was determined from the titration curves at I 0·2 in the presence and absence of the cations. The binding of Y3+ was greater than that of Ca2+. The value for the association constant, k, for the interaction with Y3+ increased with pH, from log k 2·93 at pH3·4 to log k 3·50 at pH4·4, and the number of binding sites/mol. increased from 4·6 at pH3·4 to 9·1 at pH4·4. It is proposed that the binding site consists of three carboxyl groups, but it is likely that the binding is a strong electrostatic interaction rather than a co-ordination linkage. A chondroitin sulphate–protein complex also extracted from bovine cortical bone interacted with Y3+ and Ca2+ to a similar extent as did bone sialoprotein. It is suggested that these materials are present in bone at the resting and resorbing surfaces and that they contribute to the deposition of yttrium, americium and plutonium at these sites.