Stabilization of enzymes by their specific antibodies
| Autor: | E.Y. Shami, A. Rothstein, M. Zywulko, M. Ramjeesingh |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Bioengineering
Alcohol Antigen-Antibody Complex Applied Microbiology and Biotechnology Biochemistry Antibodies chemistry.chemical_compound Freeze-drying Mice Enzyme Stability Animals Humans chemistry.chemical_classification Oligopeptide biology Specific antibody Kinetics Enzyme chemistry biology.protein Thermodynamics Rabbits Antibody Glucan 1 4-alpha-Glucosidase alpha-Amylases Biotechnology |
| Zdroj: | Enzyme and microbial technology. 13(5) |
| ISSN: | 0141-0229 |
| Popis: | In nature, increased stability of enzymes has often been found to be associated with noncovalent protein-protein interactions. Specific antibodies should be suitable for this purpose. To test this hypothesis, we used a number of model enzymes, complexed them with their specific antibodies, and exposed them and the free enzymes to low and high temperature, lyophilization, oxidation, and alcohol. The retained activity of the antibody-complexed enzymes was substantially, and in some cases dramatically, higher. In general mechanistic terms, stabilization may have been accomplished either by noncovalent antibody crosslinking of discontinuous oligopeptide chains on the surface of the enzyme, thereby increasing resistance to unfolding of the enzyme, or by physical shielding by the antibodies of vulnerable sites on the surface of the enzyme. |
| Databáze: | OpenAIRE |
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