Production of biologically active thymulin in Escherichia coli through expression of a chemically synthesized gene

A synthetic gene coding for thymulin was ligated into an expression vector (pJB 1301) and placed under lac operon control. In the recombinant clones, thymulin was expressed as part of a beta galactosidase chimeric protein which was then cleaved by cyanogen bromide. Thymulin was purified using variou...

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Bibliographic Details
Published in:Biotechnology letters 1988-03, Vol.10 (3), p.155-160
Main Authors: CALENDA, A, CORDONNIER, A, LEDERER, F, LE, D. K. H, PLEAU, J. M
Format: Article
Language:English
Subjects:
Biological and medical sciences
Biotechnology
cloning
Escherichia coli
Fundamental and applied biological sciences. Psychology
gene expression
Health. Pharmaceutical industry
Industrial applications and implications. Economical aspects
Other active biomolecules
Production of active biomolecules
thymulin
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Summary:A synthetic gene coding for thymulin was ligated into an expression vector (pJB 1301) and placed under lac operon control. In the recombinant clones, thymulin was expressed as part of a beta galactosidase chimeric protein which was then cleaved by cyanogen bromide. Thymulin was purified using various chromatography systems including gel filtration and HPLC, and was detected by radioimmunoassay (RIA). In the biological assay the purified recombinant peptide demonstrated the same zinc dependency as natural thymulin and had the same amino acid composition and primary structure.
ISSN:0141-5492
1573-6776
DOI:10.1007/BF01134818