Production of methionyl-minus ovine growth hormone in Escherichia coli and one-step purification

The overproduction of ovine growth hormone (oGH) in Escherichia coli is described, achieved in part by alteration of the codon usage for nine of the first 15 amino acids (aa) of the mature hormone. Recombinant oGH (re-oGH), representing 12% of the total cellular protein, was isolated from inclusion...

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Bibliographic Details
Published in:	Gene Vol. 122; no. 2; p. 371
Main Authors:	Adams, T E, MacIntosh, B, Brandon, M R, Wordsworth, P, Puri, N K
Format:	Journal Article
Language:	English
Published:	Netherlands 15-12-1992
Subjects:	Amino Acid Sequence Animals Base Sequence Cetrimonium Cetrimonium Compounds Cloning, Molecular DNA Escherichia coli Growth Hormone - chemistry Growth Hormone - genetics Growth Hormone - isolation & purification Methionine Molecular Sequence Data Protein Folding Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Sheep Solubility
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