[Synthesis and secretion of human atrial natriuretic factor in Escherichia coli cells].
A recombinant plasmid providing for the synthesis and secretion of the human atrial natriuretic peptide (hANP) as a C-terminal hybrid with the St. aureus protein A was constructed. The level of secretion of the chimeric proteins and their proteolytic stability were shown to depend upon the genotype of the recipient strains and the cultivation conditions. The hybrid proteins were purified by chromatography on IgG Sepharose. The presence of peptides corresponding to the hANP in the acid hydrolysates of the secreted and affinity-purified proteins was confirmed by the enzyme-linked immunoassay and analytical HPLC.
Nikolaidis
M N
MN
Parsadanian
A Sh
ASh
Pozmogova
G E
GE
El'darov
M A
MA
Anan'eva
N M
NM
Maĭsurian
N A
NA
Galoian
A A
AA
D000595:Amino Acid Sequence; D009320:Atrial Natriuretic Factor / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics*; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides; D010957:Plasmids; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D013205:Staphylococcal Protein A / Q000235:genetics
C472955:NPPA protein, human; D009838:Oligodeoxyribonucleotides; D011993:Recombinant Fusion Proteins; D013205:Staphylococcal Protein A; D009320:Atrial Natriuretic Factor
Sintez i sekretsiia predserdnogo natriĭureticheskogo faktora chelovekav kletkakh Escherichia coli.