Over expression of recombinant proteins in Escherichiacoli cytoplasm often results in the formation of insoluble inclusion bodies.
外源基因在大肠杆菌中高效表达时,通常会形成不溶性、无活性的蛋白聚集体——包涵体。
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Many recombinant proteins fail to fold into native state with activity when expressed in Escherichiacoli, instead, they often misfold and are easy to accumulate as inclusion bodies.
The recombinant plasmids containing mutant genes were transformed into the Escherichiacoli strain BL21 (DE3), and the expressed proteins were found to be water soluble after the induction of IPTG.