Process for converting fused protein into active type human motilin analogues and purifying the analogues.

摘要

There is described a process for converting a fused protein containing a tandemly repeated human motilin analogues connected through a residue of methionine between neighboring motilin analogues, which is expressed in a microorganism to biologically active motilin analogues by chemically cleaving the fused protein and purifying the biologically active motilin analogues. The fused protein expressed in the transformed microorganism is cleaved by treating the same with cyanogen bromide in an aqueous solution of formic acid. After neutralization of resulting reaction solution, the purification is carried out in combination of desalting operations and chromatography operations of a hydrophobic, ion-exchange and reversed phase chromatographies.