Acylation of amino functions of proteins with monomethoxypoly (ethylene glycol)-N-succinimide carbonate |
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Authors: | Michelle Nijs Michel Gelbcke Mohamed Azarkan Jeanne Brygier Claude Guermant Danielle Baeyens-Volant Tony Musu Claudine Paul Yvan Looze |
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Institution: | (1) Protein Chemistry Unit, Faculty of Medicine, University of Brussels, Belgium;(2) Department of Pharmaceutical Organic Chemistry, Institute of Pharmacy, University of Brussels, Belgium |
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Abstract: | Monomethoxypoly(ethylene glycol)-N-succinimide carbonate (SC-PEG) was used to prepare PEG-lysozyme, PEG-papaya proteinase III, PEG-catalase, and PEG-lactoperoxidase
conjugates. SC-PEG produced extensively modified enzymes under mild conditions (pH 7.0; 25°C) within a couple of hours. PEG-enzyme
conjugates showed equal or even greater specific activity provided that low-molecularweight substrates were used to evaluate
the biological activities. However, papaya proteinase III and lysozyme lost their proteolytic and bacteriolytic activities,
respectively, on conjugation with PEG. This was most probably because of steric factors, since no drastic conformational changes
could be detected after conjugation of these enzymes with PEG chains. Unlike these enzymes, the secondary structures of the
two hemoproteins were somewhat affected by the covalent attachment of PEG chains as shown by FTIR experiments. These results
confirmed the potential usefulness of SC-PEG, for which a novel route of synthesis making use ofN,N′-disuccinimidyl carbonate was described. |
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Keywords: | mPEG covalent attachment lysozyme catalase lactoperoxydase papaya proteinase |
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