Applied Biochemistry and Biotechnology

, Volume 11, Issue 2, pp 141–152 | Cite as

Surface modification of proteins activation of monomethoxy-polyethylene glycols by phenylchloroformates and modification of ribonuclease and superoxide dismutase

  • F. M. Veronese
  • R. Largajolli
  • E. Boccú
  • C. A. Benassi
  • O. Schiavon
Original Articles


A single-step method of activation of monomethoxy-polyethylene glycols suitable for its binding to polypeptides and proteins is proposed. Based on the reaction with 2,4,5-trichloro-phenylchloroformate orp-nitrophenylchloroformate, it gives reactive PEG-phenylcarbonate derivatives. The PEG intermediate is stable on storage, the activating group is easily quantified, and the reaction with amino acid and proteins proceeds rapidly at pH near neutrality. The PEG derivatization of enzymes with this procedure is less inactivating than those previously reported. Ribonuclease and super-oxide dismutase were modified and the effect of (a) bound polymer on clearance time in rats, (b) antibody recognition, and (c) on the enzymatic activity toward low and high molecular weight substrates were studied.

Index Entries

Monomethoxypolyethylene glycol activation surface modification of proteins Superoxide dismutase modification by polymers pharmacokinetics of polymer-modified proteins proteins, surface modification of polyethylene glycols, activation of monomethoxy- phenylchloroformates, activation of monomethoxy-polyethylene glycols by ribonuclease, modification by polymers 


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Copyright information

© The Humana Press Inc 1985

Authors and Affiliations

  • F. M. Veronese
    • 1
  • R. Largajolli
    • 1
  • E. Boccú
    • 1
  • C. A. Benassi
    • 1
  • O. Schiavon
    • 1
  1. 1.Department of Pharmaceutical Sciences (Centro di Chimica del Farmaco e dei Prodotti Biologicamente Attivi del CNR)University of PadovaPadovaItaly

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