Distribution of iron between the binding sites of transferrin in serum:
methods and results in normal human subjects
A Leibman and P Aisen
When it is incompletely saturated with iron, transferrin may exist in four
molecular forms: apotransferrin, monoferric (A) transferrin (with iron
occupying only the A site of the protein), monoferric (B) transferrin, and
diferric transferrin. By combining electrophoresis in urea-polyacrylamide
gels with crossed immunoelectrophoresis using specific antihuman transferin
antiserum, it is possible to display and estimate the concentration of each
of these four forms in normal human serum. The distribution of iron between
the binding sites of transferrin is neither random nor determined by the
relative binding strengths of transferrin's two sites. Rather, the more
weakly binding and acid-labile B site of the protein is predominantly
occupied.
Volume 53,
Issue 6,
pp. 1058-1065,
06/01/1979
Copyright © 1979 by The American Society of Hematology
