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Heterologous expression of bovine lactoferricin in Pichia methanolica.

Authors :
HaiKuan Wang
XinHuai Zhao
FuPing Lu
Source :
Biochemistry (00062979). Jun2007, Vol. 72 Issue 6, p640-643. 4p. 1 Diagram, 3 Graphs.
Publication Year :
2007

Abstract

According to the bias of codon utilization of Pichia methanolica, a fragment encoding bovine lactoferricin has been cloned and expressed in the P. methanolica under the control of the alcohol oxidase promoter, which was followed by the Saccharomyces cerevisiae α-factor signal peptide. The α-factor signal peptide efficiently directed the secretion of bovine lactoferricin from the recombinant yeast cell. The recombinant bovine lactoferricin appears to be successfully expressed, as it displays antibacterial activity (antibacterial assay). Moreover, the identity of the recombinant product was estimated by Tricine-SDS-PAGE. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00062979
Volume :
72
Issue :
6
Database :
Academic Search Index
Journal :
Biochemistry (00062979)
Publication Type :
Academic Journal
Accession number :
25558996
Full Text :
https://doi.org/10.1134/S0006297907060065