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
in English
| 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.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Plasmids
/
Recombinant Fusion Proteins
/
Humans
/
Genetic Engineering
/
Gene Expression
/
Escherichia coli
/
Genetic Vectors
/
Insulin
Language:
English
Journal:
Indian J Pathol Microbiol
Year:
2004
Type:
Article
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