Tuning substrate selectivity of a cationic enzyme using cationic polymers
Noncovalent interactions between an artificial molecular scaffold and a protein are interesting due to the possibility of reversible modulation of the activity of the protein. alpha-Chymotrypsin is a positively charged protein that has been shown to interact with negatively charged polymers. Here we...
| Publié dans: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 22(2006), 18 vom: 29. Aug., Seite 7695-700 |
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| Auteur principal: | |
| Autres auteurs: | , , |
| Format: | Article |
| Langue: | English |
| Publié: |
2006
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| Accès à la collection: | Langmuir : the ACS journal of surfaces and colloids |
| Sujets: | Journal Article Research Support, U.S. Gov't, Non-P.H.S. Cations Polymers Chymotrypsin EC 3.4.21.1 alpha-chymotrypsin Lysine K3Z4F929H6 |
| Résumé: | Noncovalent interactions between an artificial molecular scaffold and a protein are interesting due to the possibility of reversible modulation of the activity of the protein. alpha-Chymotrypsin is a positively charged protein that has been shown to interact with negatively charged polymers. Here we show that positively charged polymers are also capable of electrostatically binding to this protein. The resulting experiments show that the ability of a polymer to bind a protein does not depend only on the pI of the protein. We also realized that the variations in charge density in the polymer backbone afford different selectivities of the enzyme toward charged substrates |
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| Description: | Date Completed 21.09.2007 Date Revised 24.11.2016 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |