Production of human PTH(1-34) via a recombinant DNA technique.
The production of hPTH(1-34) by site specific chemical cleavage of [Cys35]hPTH(1-84) obtained by a biotechnology technique is described. The amino-peptide bond of S-cyanylated cysteine residues in peptides or proteins is specifically cleaved by exposure to an alkaline solution (Stark, G. R. (1977) Methods Enzymol, 47, 129-132). However, when applying this method to [Cys35]hPTH(1-84), we observed many by-products. Formation of these by-products was suppressed using a short reaction in 0.03N NaOH containing 6M urea at low temperature, and hPTH(1-34) was specifically produced. The product was indistinguishable from standard hPTH(1-34) with respect to chemical and biological characterization.
Nakagawa
S
S
Pharmaceutical Research Laboratories II, Takeda Chemical Industries, Ltd., Osaka, Japan.
Tamakashi
Y
Y
Ishibashi
Y
Y
Kawase
M
M
Taketomi
S
S
Nishimura
O
O
Fukuda
T
T
D000595:Amino Acid Sequence; D001681:Biological Assay; D006801:Humans; D008969:Molecular Sequence Data; D010281:Parathyroid Hormone / Q000737:chemistry; D010446:Peptide Fragments; D010449:Peptide Mapping; D011993:Recombinant Fusion Proteins / Q000737:chemistry
D010281:Parathyroid Hormone; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins