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. 1996 Oct 1;319(Pt 1):191–195. doi: 10.1042/bj3190191

High-yield production of functionally active human serum transferrin using a baculovirus expression system, and its structural characterization.

S A Ali 1, H C Joao 1, R Csonga 1, F Hammerschmid 1, A Steinkasserer 1
PMCID: PMC1217754  PMID: 8870668

Abstract

Recently, there has been much interest in expressing recombinant human serum transferrin (HST) and mutants thereof for structural and functional studies. We have developed a baculovirus expression system for the rapid and efficient production of large quantities of HST (> 20 mg/l). Like native HST, the recombinant protein can bind two ferric ions in the presence of bicarbonate, and is actively taken up by receptor-mediated endocytosis. Secondary structure calculations from CD measurements indicate a content of 42% alpha-helix and 28% beta-sheet. This is the first reported use of a non-mammalian expression system to produce functional HST, and will provide a practical tool to allow expression of a wide range of HST variants for mutagenesis studies.

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Selected References

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