Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2021250 | Protein Expression and Purification | 2009 | 7 Pages |
Abstract
Exendin-4 is a naturally occurring 39 amino acid peptide that is useful for the control of Type 2 diabetes. Recombinant Exendin-4, with an extra glycine at the carboxy-terminus (Exdgly), was expressed in the methylotropic yeast Pichia pastoris. A high proportion of the Exdgly molecules secreted into medium were found to be clipped, lacking the first two amino acids (His-Gly) from the N-terminus. Disruption of the P. pastoris homolog of the Saccharomyces cerevisiae dipeptidyl aminopeptidase (STE13) gene in Pichia genome resulted in a clone that expressed N-terminally intact Exdgly. Elimination of N-terminal clipping enhanced the yield and simplified the purification of Exdgly from P. pastoris culture supernatant.
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Authors
Lakshmi Prabha, Nagaraj Govindappa, Laxmi Adhikary, Ramakrishnan Melarkode, Kedarnath Sastry,