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Effects of Polyethylene Glycol Substitution on Enzyme Activity

Department of Chemistry University of Alabama in Huntsville Huntsville, AL 35899

Steven G. Shafer

Department of Chemistry University of Alabama in Huntsville Huntsville, AL 35899

J. Milton Harris

Department of Chemistry University of Alabama in Huntsville Huntsville, AL 35899

The effects of polyethylene-glycol (PEG) substitution on protein activity, us ing alkaline phosphatase as a model, have been studied. Such variables as PEG molecular weight, degree of substitution, and PEG mono- and di-functionality have been examined. Modification with the monomethyl ether of PEG 1900 (M- PEG-1900) does not alter enzyme activity until greater than 40% of the protein lysine groups are substituted, at which point increasing the degree of modifica tion gives increasing deactivation. Substitution with M-PEG-5000 gives more deactivation than does substitution with M-PEG-1900. Interestingly, modifica tion with PEG itself gives active protein conjugates in which there is little de pendence on molecular weight or degree of substitution.

Journal of Bioactive and Compatible Polymers, Vol. 2, No. 1, 49-56 (1987)
DOI: 10.1177/088391158700200103


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