Syntheses of recombinant yellowtail and flounder growth hormones in Escherichia coli.
For syntheses of recombinant yellowtail and flounder growth hormones (r-yGH and r-fGH) in E. coli, expression plasmids were constructed. The expression level of r-yGH and r-fGH in the host cells were very high, reaching 15 and 8% of the total protein, respectively. These product proteins were accumulated in inclusion bodies in the cells. The recombinant hormones were isolated from the pellets ina glutathione reduction/oxidation buffer. The refolded hormones were further purified by DEAE-Toyopearl 650M chromatography to homogeneity. The purified r-yGH and r-fGH were composed of 188 and 174 amino acid residues, respectively, having amino-terminal sequences starting with methionine. The recombinant hormones had potent growth-promoting activities on juvenile rainbow trout Salmo gairdneri in a dose-dependent manner.
Watahiki
M
M
Department of Biochemistry, Mie University School of Medicine, Japan.
Ohara
E
E
Tsuda
M
M
Shoji
K
K
Masuji
A
A
Tanaka
M
M
Yamakawa
M
M
Ushiro
H
H
Yoneda
Y
Y
Nakashima
K
K
D000818:Animals; D001483:Base Sequence; D001709:Biotechnology; D004274:DNA, Recombinant / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D005399:Fishes / Q000235:genetics; D005432:Flounder / Q000235:genetics; D005822:Genetic Vectors; D013006:Growth Hormone / Q000096:biosynthesis* / Q000235:genetics* / Q000494:pharmacology; D008969:Molecular Sequence Data; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000494:pharmacology; D014337:Trout / Q000254:growth & development
D004274:DNA, Recombinant; D011994:Recombinant Proteins; D013006:Growth Hormone