MODIFICATION OF THE ENZYMIC ACTIVITY OF TRYPSIN BY INTRAMOLECULAR CROSS-LINKS
| Autor: | W. B. Gratzer, G. H. Beaven |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
chemistry.chemical_classification
Chemical Phenomena Protein Conformation Stereochemistry Amidines Trypsin Biochemistry Benzamidine Chemistry Structure-Activity Relationship chemistry.chemical_compound Enzyme chemistry Glutaral Intramolecular force Benzene Derivatives Chromatography Gel medicine Animals Cattle Glutaraldehyde medicine.drug |
| Zdroj: | International Journal of Peptide and Protein Research. 5:215-218 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1973.tb03455.x |
| Popis: | The introduction of intramolecular cross-links into trypsin with glutaraldehyde causes inactivation of the enzyme. When the reaction is performed in the presence of the inhibitor, benzamidine, a product of enhanced activity is obtained, although the number of cross-links remains about the same. Possible cross-linking schemes to explain these effects in terms of small conformational adjustments, caused by the inhibitor, are considered. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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