[Genetic engineering of oxytocin: isolation of oxytocinoyllysine].
A hybrid protein, Il-Ox-K, was obtained from cells of E. coli TG1/pTOTEilox strain. The N-terminal sequence of this protein (63 amino acid residues) is a fragment of human interleukin-3, and the C-terminal sequence represents the full amino acid sequence of oxytocin flanked by a lysine residue. The modified oxytocinoyl-Lys containing S-sulfocysteine residues was isolated after tryptic digestion of S-sulfoderivative of the hybrid protein. The modified peptide was converted into the cyclic form containing the disulfide bonds [formula: see text]. Obtaining the oxytocinoyl-Lys proves the possibility of preparing short peptides using the microbiological synthesis.
Ovchinnikova
T V
TV
Murav'eva
T I
TI
Chupova
L A
LA
Tagaev
A A
AA
Martynova
N Iu
NIu
Miroshnikov
A I
AI
D000595:Amino Acid Sequence; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D007377:Interleukin-3 / Q000235:genetics; D008969:Molecular Sequence Data; D010121:Oxytocin / Q000031:analogs & derivatives* / Q000235:genetics* / Q000302:isolation & purification; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000302:isolation & purification*
D007377:Interleukin-3; D011993:Recombinant Fusion Proteins; C015332:oxytocin, Lys(8)-; D010121:Oxytocin