Expression of human angiotensinogen cDNA in Escherichia coli.

摘要: Human angiotensinogen cDNA clones were isolated from a human liver library. Nucleotide sequence analysis of these revealed that position 1075 in the messenger RNA, which is part PstI recognition sequence, different published (Kageyama, R., Ohkubo, H., and Nakanishi, S. (1984) Biochemistry 23, 3603-3609). This change results an altered amino acid at this corresponding protein suggests possible restriction fragment length polymorphism. The full was constructed partial ligated into isopropyl-1-thio-beta-D-galactopyranoside inducible bacterial expression vector pUC9 to develop plasmid pUCHAG27. permitted synthesis Escherichia coli. recombinant bacteria overproduced 53-kDa recognized by anti-human antibodies. greatly increased upon induction with isopropyl-1-thio-beta-D-galactopyranoside. chimeric protein, almost identical angiotensinogen, partially purified ammonium sulfate fractionation gel filtration on Sephadex G-100. kidney renin shown enzymatically cleave produce des-(angiotensin I)-angiotensinogen small polypeptide. Thus, we provide evidence synthesized through E. coli biologically active serves as substrate for renin.