Abstract
A study of regular trends in the complexation of 188Re with denatured albumin in microspheres (AMSs) prepared by dispersing a solution of human blood albumin in olive oil with continuous stirring and heating to 130°C showed that the reaction course largely depends on the concentration of the reducing agent (Sn2+) and on the temperature. With an increase in the Sn2+ concentration and temperature, the rate of the complex formation and the level of 188Re binding with AMSs regularly increase. The 188Re-AMS stability in vitro is essentially independent of the reaction mixture acidity in the pH range 3–7, whereas the stability of the labeled AMSs in vivo is influenced by pH more appreciably. Tests on laboratory animals showed that the most stable preparation was obtained at pH 5.
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