Escherichia coli-based production of recombinant ovine angiotensinogen and its characterization as a renin substrate.

ABSTRACT:

Background

Angiotensinogen (ANG) is a macromolecular precursor of angiotensin, which regulates blood pressure and electrolyte balance. ANG is specifically cleaved by renin, an aspartic protease, to initiate the angiotensin-processing cascade. Ovine ANG (oANG) from sheep plasma has been shown to be a better substrate for human renin, and it has been used in clinical renin assays. To expand the availability of oANG, we aimed to produce milligram levels of recombinant oANG using an Escherichia coli expression system.

Results

When recombinant oANG was expressed from a T7 promoter in various E. coli strains at 37 °C, it accumulated in the insoluble fraction. However, by expressing oANG at 37 °C from a tac promoter, which has weaker transcriptional activity than a T7 promoter, we

SUBMITTER: Yamashita S 

PROVIDER: S-EPMC4823841 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature