A novel approach of recombinant laterosporulin production using the N-SH2 domain of SHP-2.

ABSTRACT:

Background

The current study was aimed at evaluating the role of the N-SH2 domain of SHP-2 as a partner protein in the expression of a toxic peptide, laterosporulin (LTS). We also investigated its effects on the formation of the disulfide bond and functional folding of the peptide in vitro. The N-SH2-LTS protein was expressed as a His-tagged fusion protein, capable of undergoing enzymatic cleavage.

Results

Based on the data presented herein, the total yield of the folded fusion protein from inclusion bodies was found to be about 105 mg/l, demonstrating a high-level of heterologous expression. After enzymatic cleavage, 1.5 mg of the folded recombinant laterosporulin was obtained from each 10 mg of the fusion protein. The purity of the recombinant laterosporulin was analyzed b

SUBMITTER: Salehzadeh S 

PROVIDER: S-EPMC8529825 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature