Effects of operating parameters in in vitro renaturation of a fusion protein of human growth hormone and glutathione S transferase from inclusion body
- 30 September 2000
- journal article
- Published by Elsevier in Process Biochemistry
- Vol. 36 (1-2) , 111-117
- https://doi.org/10.1016/s0032-9592(00)00185-0
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Molten Globule Intermediate of Recombinant Human Growth Hormone: Stabilization with SurfactantsBiotechnology Progress, 1996
- Evidence for a self-associating equilibrium intermediate during folding of human growth hormoneBiochemistry, 1993
- Isolation, renaturation, and formation of disulfide bonds of eukaryotic proteins expressed in Escherichia coli as inclusion bodiesBiotechnology & Bioengineering, 1993
- Refolding of recombinant porcine growth hormone in a reducing environment limits in vitro aggregate formationFEBS Letters, 1991
- Protein Aggregation in vitro and in vivo: A Quantitative Model of the Kinetic Competition between Folding and AggregationNature Biotechnology, 1991
- Structure and Morphology of Protein Inclusion Bodies in Escherichia ColiNature Biotechnology, 1991
- Refolding and aggregation of bovine carbonic anhydrase B: quasi-elastic light scattering analysisBiochemistry, 1990
- Evidence for a molten globule state as a general intermediate in protein foldingFEBS Letters, 1990
- Solubility of different folding conformers of bovine growth hormoneBiochemistry, 1988
- Recombinant‐DNA‐derived bovine growth hormone from Escherichia coliEuropean Journal of Biochemistry, 1987