Comparative studies of manganese(II)-, nickel(II)-, zinc(II)-, copper(II)-, cadmium(II)-, and iron(III)-binding components in human cord and adult sera

Abstract

The binding of 6 trace metals, Mn(II), Ni(II), Zn(II), Cu(II), Cd(II) and Fe(III), to human cord serum was studied by Sephadex G-100 gel filtration at physiological pH, using radioisotopes as tracers. The results are compared with those obtained from adult serum. In both cord and adult sera, extensive amounts of the metals are bound to high MW proteins. Among them, Fe(III) is mostly bound to transferrin; Ni(II), Zn(II), Cu(II), and Cd(II) are bound to albumin and other macromolecules. The binding of Mn(II) either to transferrin or albumin is not resolved. Small fractions of Zn(II), Cu(II), and Cd(II) and large fractions of Mn(II) and Ni(II) were associated with low MW components of both sera. The distribution varies from metal to metal. The low MW component of the size 1500-10,000 was present in all the metals studied. Further purification of this component was attempted by DEAE-cellulose ion-exchange chromatography. The possible identity as well as the biological role played by this particular component of serum in the transport of metals in blood and across membranes is discussed.