Stabilization of concanavalin a by metal ligands
| Autor: | Ronald J. Doyle, Sandra K. Nicholson, David L. Thomasson |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Macromolecular Substances
Hydrochloride Inorganic chemistry chemistry.chemical_element Manganese Calcium Ligands Biochemistry Analytical Chemistry Metal chemistry.chemical_compound Drug Stability Concanavalin A Guanidine Binding Sites Glycogen biology Precipitation (chemistry) Organic Chemistry Temperature General Medicine Kinetics chemistry visual_art visual_art.visual_art_medium Biophysics biology.protein Protein Binding |
| Zdroj: | Carbohydrate Research. 46:111-118 |
| ISSN: | 0008-6215 |
| DOI: | 10.1016/s0008-6215(00)83535-1 |
| Popis: | Metal-free concanavalin A is readily and irreversibly inactivated by temperatures above 60°. Manganese ion completely prevents the thermal aggregation of the protein at 60 and 70°, and partially protects at 80°, but shows no protective properties at 90°. Manganese protection against thermal aggregation was found to be maximal at pH 4-8. The precipitation between glycogen and Mn 2+-stabilized concanavalin A is partially inhibited at temperatures > 30°, but can be reversed by cooling to room temperature. Manganese ion also partially reverses the inhibition of concanavalin A-glycogen complex-formation by protein denaturants and by saccharides. At 20°, calcium ion plus Mn2+ prevents the aggregation of metal-free concanavalin A induced by guanidine hydrochloride. The results show, contrary to conclusions from previous studies, that concanavalin A is a highly stable protein when supplemented with Mn2+ and Ca2+. |
| Databáze: | OpenAIRE |
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