Skip to main content
SpringerLink
Log in

Chemical modification of l-asparaginase from Escherichia coli with a modified polyethyleneglycol under substrate protection conditions

  • Published:
Biotechnology Letters Aims and scope Submit manuscript

Abstract

l-Asparaginase was chemically modified with 2,4-bis(O-methoxypolyethyleneglycol)-6-chloro-S-triazine (mPEG2) in the presence of l-asparagine. Optimal modification was performed under the condition that the molar ratio of mPEG2/-NH2 is 10. The modified enzyme retained 33% of initial enzymatic activity with complete abolishment of immunogenicity. In vitro half-life increment from 4.6 h to 33 h has been obtained.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Ashihara Y, Kono T, Yamazaki S, Inada Y (1978) Modification of E. coli L-asparaginase with polyethylene glycol: disappearance of binding ability to anti-asparaginase serum. Biochem. Biophys. Res. Commun. 83: 385–391.

    Google Scholar 

  • Maita T, Morokuma K, Matsuda G (1974) Amino acid sequence of L-asparaginase from Escherichia coli. J. Biochem. 76: 1351–1354.

    Google Scholar 

  • Matsushima A, Nishimura H, Ashihara Y, Yokota Y, Inada Y (1980) Modification of E. coli asparaginase with 2,4-bis(O-methoxypolyethyleneglycol)-6-chloro-S-triazine (activated PEG2). Chem. Lett. 103: 773–776.

    Google Scholar 

  • Matsuyama H, Taguchi R, Ikezawa H (1991) Phospholipase D modified with a polyethylene glycol derivative. Chem. Pharm. Bull. 39: 743–746.

    Google Scholar 

  • Qian GQ, Ma JB, Zhou JY, He BL (1997) Chemical modification of E. coli L-asparaginase with poly(N-vinylpyrrolidone-co-maleic anhydride). React. Funct. Polym. 32: 117–121.

    Google Scholar 

  • Roberts MJ, Bentley MD, Harris JM (2002) Chemistry for peptide and protein PEGylation. Adv. Drug Deliv. Rev. 54: 459–476.

    Google Scholar 

  • Soares AL, Guimarães GM, Polakiewicz B, Pitombo RNM et al. (2002) Effects of polyethylene glycol attachment on physicochemical and biological stability of E. coli L-asparaginase. Inter. J. Pharm. 237: 163–170.

    Google Scholar 

  • Uren JR, Hargis BJ, Beardsley P (1982) Immunological and pharmacological characterization of poly-DL-alanyl-modified Erwinia carotovora L-asparaginase. Cancer Res. 42: 4068–4071.

    Google Scholar 

  • Wileman T, Foster RL, Elliot PNC (1986) Soluble asparaginasedextran conjugates show increased circulatory persistence and lowered antigen reactivity. J. Pharm. Pharmacol. 38: 264–271.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. State Key Laboratory of Bioreactor Engineering, Research Institute of Biochemistry, East China University of Science and Technology, Shanghai, 200237, P.R. China

    Jian-Feng Zhang, Ling-Yang Shi & Dong-Zhi Wei

Authors
  1. Jian-Feng Zhang
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ling-Yang Shi
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Dong-Zhi Wei
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Zhang, JF., Shi, LY. & Wei, DZ. Chemical modification of l-asparaginase from Escherichia coli with a modified polyethyleneglycol under substrate protection conditions. Biotechnology Letters 26, 753–756 (2004). https://doi.org/10.1023/B:BILE.0000024100.49716.3d

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/B:BILE.0000024100.49716.3d

Search

Navigation