High–Level Expression, Efficient Secretion and Folding of Human Growth Hormone in Escherichia coli
- 1 November 1986
- journal article
- Published by Springer Nature in Bio/Technology
- Vol. 4 (11) , 991-995
- https://doi.org/10.1038/nbt1186-991
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Technology spurt resolves growth hormone problem, ends shortageJAMA, 1986
- Synthesis and secretion of human epidermal growth factor by Escherichia coli.Proceedings of the National Academy of Sciences, 1985
- Isolation and Purification of Protein Granules from Escherichia coli Cells Overproducing Bovine Growth HormoneBio/Technology, 1985
- Periplasmic production of correctly processed human growth hormone in Escherichia coli: natural and bacterial signal sequences are interchangeableGene, 1985
- Bacteria mature preproinsulin to proinsulin.Proceedings of the National Academy of Sciences, 1980
- Secretion of beta-lactamase requires the carboxy end of the proteinCell, 1980
- Eukaryotic signal sequence transports insulin antigen in Escherichia coli.Proceedings of the National Academy of Sciences, 1980
- Human Growth Hormone: Complementary DNA Cloning and Expression in BacteriaScience, 1979
- [6] Improved phosphotriester method for the synthesis of gene fragmentsPublished by Elsevier ,1979
- Human pituitary growth hormone. XXI. Physicochemical investigations of the native and reduced-alkylated proteinBiochemistry, 1969