Refolding of porcine growth hormone from inclusion bodies of Escherichia coli

Baranauskaitė, Laima; Sereikaitė, Jolanta; Gedminienė, Genovaitė; Bumelienė, Žana; Bumelis, Vladas Algirdas

doi:10.1080/10242420500175820

Use this URL to cite this publication: https://hdl.handle.net/20.500.14911/139262

Refolding of porcine growth hormone from inclusion bodies of Escherichia coli

Details

Publication Type (CRIS)

Straipsnis Web of Science duomenų bazėje / Article in Web of Science database (S1a)

Publication Type (eLABa)

Straipsnis Web of Science DB / Web of Science DB article (S1)

Author(s)

Author	Affiliation
Baranauskaitė, Laima	Fundamentinių mokslų fakultetas / Faculty of Fundamental Sciences (10)
Sereikaitė, Jolanta	Chemijos ir bioinžinerijos katedra / Department of Chemistry and Bioengineering (1032)
Gedminienė, Genovaitė	Chemijos ir bioinžinerijos katedra / Department of Chemistry and Bioengineering (1032)
Bumelienė, Žana	Chemijos ir bioinžinerijos katedra / Department of Chemistry and Bioengineering (1032)
Bumelis, Vladas Algirdas	Chemijos ir bioinžinerijos katedra / Department of Chemistry and Bioengineering (1032)

Title

Refolding of porcine growth hormone from inclusion bodies of Escherichia coli

[en]

Laima Baranauskaite, Jolanta Sereikaite, Genovaite Gedminiene, Zana Bumeliene, Vladas-Algirdas Bumelis

Is part of

Biocatalysis and Biotransformation

Published In

Year	Volume	Issue	Start Page	End Page
2005	23	3-4	185	189

Publisher

Abingdon : Taylor & Francis

Publisher (trusted)

Taylor & Francis

Referenced in Database(s)(DBs)

Science Citation Index Expanded (Web of Science)

Compendex

Academic Search Premier

Extent

p. 185-189

URI

URI
https://hdl.handle.net/20.500.14911/139262

DOI

10.1080/10242420500175820

Science / Art Area

Gamtos mokslai / Natural Sciences (N)

Field of Science / Art

Chemija / Chemistry (N003)

Abstract (en)

Escherichia coli cells expressing porcine growth hormone were grown in a batch fermentation process. The expression level was estimated to be nearly 40% of the total cellular protein after 2–3 h of induction with 1 mM isopropyl β-d-thiogalactoside. Porcine growth hormone expressed as inclusion bodies was solubilized in 8 M urea. Refolding conditions following a dilution protocol in the presence of β-mercaptoethanol or using a glutathione pair were tested. Reverse phase-HPLC was applied to distinguish oxidized, misfolded and reduced forms of the hormone. A ratio of reduced to oxidized glutathione equal to 2/1 was chosen to avoid the formation of misfolded forms at high protein concentration.