| Autor: |
Walker, John M., Vulfson, Evgeny N., Holland, Herbert L., Halling, Peter J., Matsushima, Ayako, Kodera, Yoh, Hiroto, Misao, Nishimura, Hiroyuki, Inada, Yuji |
| Zdroj: |
Enzymes in Nonaqueous Solvents; 2001, p49-64, 16p |
| Abstrakt: |
Chemical modification of proteins with polyethylene glycol (PEG), a nontoxic, nonimmunogenic, and amphipathic polymer, has been extensively studied for the purpose of applying proteins to biomedical and biotechnological processes (1-9). In the biomedical field, the purpose of the chemical modification of enzymes with PEG includes the reduction of their immunoreactivity and immunogenicity as well as the prolongation of the plasma half-life of the modified enzymes (5,10-13). Several PEG enzymes such as PEG-ADA (adenosine deaminase) and L-asparaginase are now approved by the U.S. Food and Drug Administration (FDA). In the biotechnological field, the purpose of the chemical modification of enzymes with PEG includes the preparation of novel catalysts, PEG enzymes, which are soluble and active in organic solvents (14,15). [ABSTRACT FROM AUTHOR] |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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