Direct expression in Escherichia coli of a DNA sequence coding for human growth hormone
- 1 October 1979
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 281 (5732) , 544-548
- https://doi.org/10.1038/281544a0
Abstract
DNA coding for human growth hormone was constructed by using chemically synthesised DNA in conjunction with enzymatically prepared cDNA. This ‘hybrid’ gene was expressed in Escherichia coli under the control of the lac promoter. A polypeptide was produced having the size and immunological properties characteristic of mature human growth hormone.This publication has 28 references indexed in Scilit:
- Synthesis of growth hormone by bacteriaNature, 1978
- Phenotypic expression in E. coli of a DNA sequence coding for mouse dihydrofolate reductaseNature, 1978
- Synthesis of an ovalbumin-like protein by Escherichia coli K12 harbouring a recombinant plasmidNature, 1978
- Maximizing gene expression on a plasmid using recombination in vitroCell, 1978
- Expression in Escherichia coli of a Chemically Synthesized Gene for the Hormone SomatostatinScience, 1977
- Construction and analysis of recombinant DNA for human chorionic somatomammotropinNature, 1977
- Nucleotide sequence and amplification in bacteria of structural gene for rat growth hormoneNature, 1977
- Rat Insulin Genes: Construction of Plasmids Containing the Coding SequencesScience, 1977
- E. coli lactose operon ribosome binding siteNature, 1974
- Intracellular location of newly synthesized growth hormoneExperimental Cell Research, 1973