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. 1978 Apr 1;171(1):73–78. doi: 10.1042/bj1710073

Characterization of monoferric fragments obtained by tryptic cleavage of bovine transferrin.

J H Brock, F R Arzabe, N E Richardson, E V Deverson
PMCID: PMC1184134  PMID: 646825

Abstract

1. The electrophoretically fast (F) and slow (S) fragments obtained by tryptic cleavage of bovine iron-saturated transferrin differed in carbohydrate content and peptide 'maps'. 2. A fragment capable of binding one Fe3+ ion per molecule was isolated after brief tryptic digestion of bovine apotransferrin and shown closely to resemble the S fragment obtained from the iron-saturated protein. 3. Fragments F and S are probably derived from the N- and C-terminal halves of the transferrin molecule respectively. 4. Bovine transferrin could donate iron to rabbit reticulocytes, but the monoferric fragments possessed little iron-donating ability.

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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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