[Expression in Escherichia coli cells of the nucleotide sequence of DNA coding for the bovine lipotropic hormone].
A cDNA fragment of bovine proopiomelanocortin coding for beta-lipotropic hormone was joined with a promoter and ribosome binding site of B. amyloliquefaciens and cloned in E. coli in pBR 327 plasmid. The level of beta-lipotropin synthesis in bacterial cells transformed by the obtained plasmid was estimated immunochemically. The level of beta-lipotropin production was shown to be 5 mg per liter of bacterial culture.
Beklemishev
A B
AB
Golovin
S Ia
SIa
Il'ichev
A A
AA
Mamaev
L V
LV
Krasnykh
V N
VN
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002417:Cattle; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics; D005813:Genes, Synthetic; D008969:Molecular Sequence Data; D010957:Plasmids; D011333:Pro-Opiomelanocortin / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics; D008083:beta-Lipotropin / Q000235:genetics*
D012333:RNA, Messenger; D011333:Pro-Opiomelanocortin; D004247:DNA; D008083:beta-Lipotropin
Ekspressiia v kletkakh Escherichia coli nukleotidnoĭ posledovatel'nosti DNK, kodiruiushcheĭ lipotropnyĭ gormon byka.