EMAIL THIS PAGE TO A FRIEND

European journal of biochemistry

Expression of atrial natriuretic factor as a cleavable fusion protein with chloramphenicol acetyltransferase in Escherichia coli.


PMID 2968246

Abstract

Recombinant fusion proteins containing human atrial natriuretic factor, ANF(1-28) joined to chloramphenicol acetyltransferase (CAT) via cleavable linker sequences have been produced in Escherichia coli. The linker sequences were designed to allow the release of authentic ANF(1-28) following proteolytic cleavage by enterokinase or thrombin, or chemical cleavage with 2-(2-nitrophenylsulphenyl)-3-methyl-3'-bromoindolenine. Proteins, containing ANF(1-28) fused to the carboxyl-terminal region of CAT (using the ScaI restriction site in the cat gene), were largely soluble in E. coli and were obtained in higher yield than analogues containing ANF(1-28) linked to shorter CAT sequences. The longer derivatives also retained CAT activity allowing subsequent purification by affinity chromatography.

Related Materials

Product #

Image

Description

Molecular Formula

Add to Cart

B4651
3-Bromo-3-methyl-2-(2-nitrophenylthio)-3H-indole, ≥85%
C15H11BrN2O2S