These data suggest that inherent properties of bacterial expression strains may also determine the fate of expressed proteins. Factors such as chaperonins and their role in protein folding to native and denatured forms during overexpression and heat shock conditions may be related to inclusion bodies. Conclusion Multiple forms of Rat and Human Sulfotransferase can be readily expressed in bacterial cytosol and purified. Overexpression of some forms of sulfotransferases stimulates the formation of inclusion bodies. The formation can not be related to primary or secondary protein structure and is not always consistent, e.g., HST 20 is expressed in inclusion bodies of some clones of E.Coli and in cytosol of other clones of the same bacterial strain.
Mechanisms underlying the formation of inclusion bodies remain ill defined and variable.
European Journal of Drug Metabolism and Pharmacokinetics. Rose, Burkhard and Sandler, Chris. Weinshilboum, Richard M. Otterness, Diane M., Aksoy, Ibrahim, Wood, Thomas, Her, Cheng Tos, and Raftogianis, Rebecca. The process of sulfonation is critical for the metabolism of many chemical substances. The Mono-Q column is an anion exchange column that separates HST 40 from other proteins having different electrical charges.