Abstract
Electrophoretically separated rabbit serum albumin is essentially in a monomeric form, whereas old freeze-dried albumin or fresh albumin oxidized by chloramine T, at pH 5.1, shows a number of polymers. The monomer, the dimer, the trimer, the tetramer, and the polymers of old freeze-dried rabbit serum 131I-albumin have been separated by gel filtration on Sephadex G-200 and, by determining the relative specific activities, a decrease of radioactivity has been shown in the polymeric albumin. The albumin components have been characterized by agar and starch gel electrophoresis and by double diffusion in agar gel in order to ascertain the purity and the identity with the monomeric albumin. Having excluded depolymerization of 131I-albumin aggregates in vivo, the biological behavior of rabbit 131I-albumin, either in monomeric or in polymeric form, was examined. The results indicate a progressive shorter half-life and an increase in the eliminated radioactivity as the degree of polymerization increases.
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