Characterization of Recombinant Salmon Growth Hormone I Expressed in Escherichia coli.
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CONSTRUCTION OF RECOMBINANT PLASMIDS FOR PERIPLASMIC EXPRESSION OF HUMAN GROWTH HORMONE IN ESCHERICHIA COLI UNDER T7 AND LAC PROMOTERS
In order to study the periplasmic expression of human growth hormone (hGH) in Escherichia coli, the related cDNA was inserted in two expression plasmids carrying pelB signal peptide, one with lac bacterial promoter and the other with a bacteriophage T7-based promoter. The recombinant plasmids were moved to TG1 and BL21 strains of E. coli, respectively. To induce the expression systems, IPTG and...
متن کاملPurification and biochemical characterization of recombinant human placental growth hormone produced in Escherichia coli.
The hGH-V (or hGH-2) gene codes for human placental growth hormone (hPGH). Secretion of hPGH is continuous, in contrast with the pulsed secretion of pituitary growth hormone (hGH) which it progressively replaces in the maternal bloodstream. hGH-V cDNA has previously been cloned and isolated. Analysis of its nucleotide sequence has revealed a 191-residue protein, hPGH, differing from hGH at 13 p...
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The human granulocyte-macrophage colony stimulation factor (hGM-CSF) gene was cloned in the pET 23a( +) expression vector under the control of strong bacteriophage T7 transcription and translation signals. The hGM-CSF gene was transferred into E. coli strainBL21 (DE3)pLysS andIPTG was used for induction of GM-CSF gene. Production of the target protein was obtained as revealed by ELISA and ...
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Background: Pivotal roles of Nerve growth factor (NGF) in the development and survival of both neuronal and non-neuronal cells indicate its potential for the treatment of neurodegenerative diseases. However, investigation of NGF deficits in different diseases requires the availability of properly folded human b-NGF. In previous studies bacterial expression of hNGF demonstrated the feasibility o...
متن کاملCloning and expression of cDNA for salmon growth hormone in Escherichia coli.
cDNA clones encoding chum salmon (Oncorhynchus keta) growth hormone (sGH) have been isolated from a cDNA library prepared from chum salmon pituitary gland poly(A)(+) RNA. Synthetic oligodeoxynucleotide mixtures based on amino acid residues 23-28 of sGH were used as hybridization probes to select recombinant plasmids carrying the sGH coding sequence. The complete nucleotide sequence of sGH cDNA ...
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ژورنال
عنوان ژورنال: NIPPON SUISAN GAKKAISHI
سال: 1991
ISSN: 1349-998X,0021-5392
DOI: 10.2331/suisan.57.1759