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

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.

SUBMITTER: Ali SA 

PROVIDER: S-EPMC1217754 | biostudies-other | 1996 Oct

REPOSITORIES: biostudies-other