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% α-helix and 28% β-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.
High-yield production of functionally active human serum transferrin using a baculovirus expression system, and its structural characterization
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
- Cite Icon Cite
Stuart A. ALI, Heidi C JOAO, Robert CSONGA, Franz HAMMERSCHMID, Alexander STEINKASSERER; High-yield production of functionally active human serum transferrin using a baculovirus expression system, and its structural characterization. Biochem J 1 October 1996; 319 (1): 191–195. doi: https://doi.org/10.1042/bj3190191
Download citation file: