Search results

Search:
in the keywords: inclusion bodies

Sort By:

Limit search:

Escherichia coli small heat shock proteins IbpA/B enhance activity of enzymes sequestered in inclusion bodies.

100%

Kuczyńska-Wiśnik D., Żurawa-Janicka D., Narkiewicz J., Kwiatkowska J., Lipińska B., Laskowska E.

vol. 51

issue 4

925-931

Escherichia coli small heat shock proteins, IbpA/B, function as molecular chaperones and protect misfolded proteins against irreversible aggregation. IbpA/B are induced during overproduction of recombinant proteins and bind to inclusion bodies in E. coli cells. We investigated the effect of ΔibpA/B mutation on formation of inclusion bodies and biological activity of enzymes sequestered in the aggregates in E. coli cells. Using three different recombinant proteins: Cro-β-galactosidase, β-lactamase and rat rHtrA1 we demonstrated that deletion of the ibpA/B operon did not affect the level of produced inclusion bodies. However, in aggregates containing IbpA/B a higher enzymatic activity was detected than in the IbpA/B-deficient inclusion bodies. These results confirm that IbpA/B protect misfolded proteins from inactivation in vivo.

Refine search results

1 Acta Biochimica Polonica

1 2004

1 Kuczyńska-Wiśnik D.

1 Kwiatkowska J.

1 Laskowska E.

1 Lipińska B.

1 Narkiewicz J.

1 Żurawa-Janicka D.

Search results

Escherichia coli small heat shock proteins IbpA/B enhance activity of enzymes sequestered in inclusion bodies.