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Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Expression and purification of recombinant human apolipoprotein C-I in Pichia pastoris
Manman Su1, Yulai Zhou, Dingding Wang
1Department of Biological Engineering, College of Pharmacy, Jilin University, 1266 Fu Jin Road, Changchun 130021, China.
Abstract:
Apolipoprotein C-I (ApoC-I) is a small, basic apolipoprotein which is mainly secreted by the liver as a component of triglyceride-rich lipoproteins and high density lipoproteins whose importance in plasma lipoprotein metabolism is increasingly evident. At present, the only way to obtain native ApoC-I is separating it from human plasma. The methods have some restrictions on source, the complicated technology, the potential infections and a high cost which limits the research and application of native ApoC-I. Because of its small size, ApoC-I has previously been prepared by peptide synthesis which is also limited by a high cost. Therefore, in this study, a Pichia pastoris expression system was first used to obtain a high level expression of secreted, recombinant human ApoC-I (rhApoC-I).
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