Kinetics of inclusion body formation and its correlation with the characteristics of protein aggregates in Escherichia coli.

ABSTRACT: The objective of the research was to understand the structural determinants governing protein aggregation into inclusion bodies during expression of recombinant proteins in Escherichia coli. Recombinant human growth hormone (hGH) and asparaginase were expressed as inclusion bodies in E.coli and the kinetics of aggregate formation was analyzed in details. Asparaginase inclusion bodies were of smaller size (200 nm) and the size of the aggregates did not increase with induction time. In contrast, the seeding and growth behavior of hGH inclusion bodies were found to be sequential, kinetically stable and the aggregate size increased from 200 to 800 nm with induction time. Human growth hormone inclusion bodies showed higher resistance to denaturants and proteinase K degradation in comparison to

SUBMITTER: Upadhyay AK 

PROVIDER: S-EPMC3315509 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature