Letter | Published:

Boric Acid-induced Heterogeneity of Conalbumin by Starch-gel Electrophoresis

Naturevolume 199pages11841186 (1963) | Download Citation



MULTIPLE molecular forms of conalbumin1, the iron-binding component of avian egg white, have been described by numerous investigators under a variety of experimental conditions. In the original purification of conalbumin, Longsworth et al.2 identified two components, the relative proportions of which were dependent on pH. Afterwards, by starch-gel electrophoresis, Lush3 identified two, and occasionally three, iron-binding proteins in native egg white, as did Williams4 and Ogden et al.5. In each of these cases3–5, the slower migrating of the two components was the more intense; in the latter investigations4,5 a corresponding heterogeneity was observed in transferrin, the iron-binding protein in the serum of the animal. Thus, in the chicken, as in other species, including man6, primates7, cattle8,9, bison10, horses11, and mice12, a single transferrin allele appears to determine the synthesis of more than one molecular species of transferrin. Ultracentrifugal investigations on purified cattle transferrins indicate that the multiple bovine components do not represent a polymer series13.

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  1. The Rockefeller Institute, New York City



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