The invention discloses a soluble expression and purification method of recombinant
human bone morphogenetic
protein in a prokaryotic
system. A
gene sequence of a recombinant
human bone morphogenetic
protein (rhBMP) is spliced at the 3'terminal of a His-
Linker-GB1
gene sequence, inserted into a
prokaryotic expression system expression vector and transferred into a prokaryotic
competent cell to be highly expressed in the
cell in a soluble form, and finally, the expressed His-
Linker-GB1-BMP
fusion protein does not need to be subjected to inclusion body renaturation, so that the recombinant
human bone morphogenetic
protein (rhBMP) is obtained. The high-purity
fusion protein can be obtained through one-step
metal chelating
chromatography (adsorption-
elution mode), and the GB1 tag has small molecular weight and hardly affects the
spatial structure and
biological activity of rhBMP, so that the situation that an inclusion body is formed by expression of rhBMP in a traditional
escherichia coli
system and expression is performed in a structure-free and activity-free inclusion body form is avoided, and the expression efficiency is greatly improved. The method is simple and convenient to operate, is suitable for large-scale amplification, and has the characteristics of short period, high purity, stable process and the like.