Abstract
Human serum albumin in aqueous solution was irradiated with 7 Mrads of60 Co gamma rays in the presence of atmospheric oxygen, and analyzed by sedimentation velocity techniques. The radiation-polymerized material exhibited a continuous polydispersion, with the most abundant fraction between 1.3 and 1.7× 106 daltons, thus being equivalent to 19-25 monomeric albumin units. Monomeric albumin could not be detached by treatment with: 8 M urea, reduction and alkylation, and 1 M hydroxylamine-singly or in combination; nor was there a major decrease of sedimentation constants effected by these treatments. It is concluded that the following are not involved in cross linkages stabilizing the radiation-polymerized albumin: noncovalent bonds, disulfide bridges, simple ester, thioester, and imide bonds.
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