Overexpression for commercial production of recombinant human insulin as A-chain and B-chain fusion protein in Escherichia coli through genetically engineered plasmids.
Indian J Pathol Microbiol
;
2004 Oct; 47(4): 569-73
Article
Dans Anglais
| IMSEAR
| ID: sea-75711
ABSTRACT
The construction of expression vectors encoding either the human insulin A- or B-chains fused to a synthetic peptide and the temperature-induced expression of the recombinant genes in Escherichia coli are reported. Using this two-chain approach we also describe the separate isolation of the insulin A- and B-chains from inclusion bodies and their subsequent assembly into native human insulin. The expression yields about 600 mg of the insulin B-chain per litre of culture. Under similar conditions the expression yield of the insulin A-chain corresponds to approximately 500 mg per litre of culture. This is the highest yield from shake flask experiments.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
Sujet Principal:
Plasmides
/
Protéines de fusion recombinantes
/
Humains
/
Génie génétique
/
Expression des gènes
/
Escherichia coli
/
Vecteurs génétiques
/
Insuline
langue:
Anglais
Texte intégral:
Indian J Pathol Microbiol
Année:
2004
Type:
Article
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