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. 1968 Jun;108(1):69–74. doi: 10.1042/bj1080069

The isoelectric fractionation of hen's-egg ovotransferrin

R V Wenn 1, J Williams 1
PMCID: PMC1198770  PMID: 5657452

Abstract

1. Hen ovotransferrin was examined by isoelectric fractionation. 2. The major component observed in starch-gel electrophoresis can be isolated from the minor component. 3. When non-saturating amounts of iron are added to ovotransferrin, isoelectric fractionation demonstrates the existence of three molecular species corresponding to the metal-free protein, the one-iron-atom–protein complex and the two-iron-atoms–protein complex. 4. Isoelectric fractionation of human serum labelled with 59Fe suggests that the transferrin of normal human serum also exists as metal-free protein, the one-iron-atom–protein complex and the two-iron-atoms–protein complex. 5. It is concluded that the binding constants for the first and second iron atoms are similar.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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