Characterization of inclusion bodies in recombinant Escherichia coli producing high levels of porcine somatotropin
- 1 April 1993
- journal article
- Published by Elsevier in Journal of Biotechnology
- Vol. 28 (2-3) , 313-320
- https://doi.org/10.1016/0168-1656(93)90179-q
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Removal of a Proteolytic Activity Associated with Aggregates Formed from Expression of Creatine Kinase in Escherichia coli Leads to Improved Recovery of Active EnzymeNature Biotechnology, 1990
- [20] Solubilization of protein aggregatesPublished by Elsevier ,1990
- Synthesis and sequence-specific proteolysis of a hybrid protein (colicin A :: growth hormone releasing factor) produced in Escherichia coliGene, 1989
- Methods for increasing the resolution of two-dimensional protein electrophoresisAnalytical Biochemistry, 1988
- Direct Expression of Bordetelia pertussis Toxin Subunits to High Levels in Escherichia coliNature Biotechnology, 1988
- Formation of recombinant protein inclusion bodies in Escherichia coliTrends in Biotechnology, 1988
- Properties of inclusion bodies from recombinant Escherichia coliBiochemical Society Transactions, 1988
- Recombinant‐DNA‐derived bovine growth hormone from Escherichia coliEuropean Journal of Biochemistry, 1987
- The purification of eukaryotic polypeptides synthesized in Escherichia coliBiochemical Journal, 1986
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970