Literature DB >> 8185633

Production of human PTH(1-34) via a recombinant DNA technique.

S Nakagawa1, Y Tamakashi, Y Ishibashi, M Kawase, S Taketomi, O Nishimura, T Fukuda.   

Abstract

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.

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Year:  1994        PMID: 8185633     DOI: 10.1006/bbrc.1994.1653

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

1.  A novel methodology for assignment of disulfide bond pairings in proteins.

Authors:  J Wu; J T Watson
Journal:  Protein Sci       Date:  1997-02       Impact factor: 6.725

2.  High-level production of recombinant human parathyroid hormone 1-34.

Authors:  Y Suzuki; M Yabuta; K Ohsuye
Journal:  Appl Environ Microbiol       Date:  1998-02       Impact factor: 4.792

3.  Optimization and applications of CDAP labeling for the assignment of cysteines.

Authors:  Gary D Pipes; Andrew A Kosky; Jeffrey Abel; Yu Zhang; Michael J Treuheit; Gerd R Kleemann
Journal:  Pharm Res       Date:  2005-07-22       Impact factor: 4.200

  3 in total

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