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PMID: 3007060 Published · ppublish English Journal Article

A general method for retrieving the components of a genetically engineered fusion protein.

DNA (Mary Ann Liebert, Inc.) ·Vol. 5 ·No. 1 ·1986-02-00 ·Pages 11-20

Szoka PR, Schreiber AB, Chan H, Murthy J

Abstract

Escherichia coli expression vectors encoding an acid-labile aspartyl-proline (Asp-Pro) dipeptide bridging two protein sequences were constructed and used to synthesize two different bovine growth hormone (bGH) fusion proteins. The codons GAT-CCX coding for Asp-Pro are provided by the recognition site for Bam HI (GGATCC). Treatment of the bGH fusion proteins at low pH in the presence of guanidine hydrochloride releases the bGH moiety from the fusion protein. The release of the bGH from the fusion protein specifically requires the Asp-Pro dipeptide linking the bGH sequence to the fusion protein. The bGH released from the fusion protein retains anti-bGH immunoreactivity as well as the ability to bind to growth hormone receptor in vitro.

MeSH Terms
Acids Amino Acid Sequence Animals Cattle DNA Restriction Enzymes/metabolism Deoxyribonuclease BamHI Escherichia coli/genetics Genetic Engineering/methods Growth Hormone/genetics Hydrolysis Receptors, Cell Surface/metabolism Receptors, Somatotropin Recombinant Proteins/genetics Tryptophan/genetics
Chemicals
Acids Receptors, Cell Surface Receptors, Somatotropin Recombinant Proteins Tryptophan Growth Hormone DNA Restriction Enzymes Deoxyribonuclease BamHI
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Szoka P R
Schreiber A B
Chan H
Murthy J
Article Info
Journal
DNA (Mary Ann Liebert, Inc.)
Abbr.
DNA
ISSN
0198-0238
Published
1986-02-00
Pages
11-20
Language
English
Region
United States
NLM ID
8302432
Subset
IM
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