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Chemical modification of proteins with polyethylene glycols

  • Y. Inada
  • A. Matsushima
  • M. Hiroto
  • H. Nishimura
  • Y. Kodera
Chapter
Part of the Advances in Biochemical Engineering/Biotechnology book series (ABE, volume 52)

Abstract

Proteins as well as bioactive substances were coupled with two types of polyethylene glycol (PEG) derivatives, one with a chain-shaped form, 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine (activated PEG2), and the other with a comb-shaped form, copolymer of PEG and maleic anhydride (activated PM). This modification technique eliminated some of the drawbacks of the native proteins and bioactive substances and also endowed them with new functions. l-Asparaginase and bovine serum albumin caused a reduction of immunoreactivity toward their antibodies and a prolongation of the clearance time through this modification. The modified lipase catalyzed the reverse reaction of hydrolysis, ester synthesis and ester exchange reactions in the hydrophobic media. This technique was further extended to various kinds of bioactive substances to form magnetic urokinase, PEG2-melanin and chlorophyll-bentonite conjugates. These phenomena have been discussed in relation to the structures of the modifiers, PEGs and PMs.

Keywords

Polyethylene Glycol Maleic Anhydride Clearance Time Pentanoic Acid Ester Synthesis 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 1995

Authors and Affiliations

  • Y. Inada
    • 1
  • A. Matsushima
    • 1
  • M. Hiroto
    • 1
  • H. Nishimura
    • 1
  • Y. Kodera
    • 1
  1. 1.Toin Human Science and Technology Center, Department of Materials Science and TechnologyToin University of YokohamaYokohamaJapan

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