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Updated: May 5, 2026
Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Isolation, Purification, and Structural-Functional Analysis of Recombinant Human Transferrin Produced by the
R Yu Popov1,2, E D Nikolskaya3, T K Aliev4,5
1National Research Centre "Kurchatov Institute", Moscow, Russia. poprom@outlook.com.
Abstract:
A recombinant modified human transferrin (N413D and N611D) was produced by the Pichia pastoris strain pPIC9pGAPZalpha-short_hTFNG (Yst-TFNG2). A multi-step protocol for isolation and purification of recombinant transferrin was developed achieving the target protein yield of 70.29% and a purity of at least 95%. Structural correspondence of the recombinant transferrin to the natural protein was confirmed by mass spectrometry and circular dichroism analysis. Functional analysis demonstrated the protein's ability to bind and release iron ions, as well as support the proliferation of eukaryotic cells.
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