Darcel C L
Comp Biochem Physiol B. 1983;76(3):423-7. doi: 10.1016/0305-0491(83)90269-9.
An extract of the livers of normal chickens (N) and chickens (Eb) infected with avian erythroblastosis virus (EbV) contained a small molecular weight protein (SMWP, mol. wt 11,000). When the extract was not dehaeminized, SMWP in agarose electrophoresis was shown to have peroxidase activity probably due to the presence of haem. When this non-dehaeminized extract was chromatographed on Con-A Sepharose neither SMWP nor an antigen (EbAg) present in Eb livers were retained. The association of EbAg with SMWP is still unexplained. Immunoelectrophoresis shows a reaction of identity between chicken SMWP and serum albumin. Chicken SMWP is thus not a beta 2-microglobulin. The finding of an immunological relationship between SMWP and albumin confirms the biochemical homology of SMWP with serum albumin in terms of amino acid residues. It has been suggested that SMWP may be a precursor or fragment of albumin but the possibility of its being a distinct entity, a microalbumin, should not be discounted.