Heparin and Concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity
A systematic study of the role of the Ca2+ and Mn2+ ions on the interaction between heparin and Concanavalin A was carried out. The protein was demetallized, and complex formation was followed by a light scattering assay. In the absence of ions no visible interaction was detected. Maximum activity w...
Guardado en:
| Autor principal: | |
|---|---|
| Publicado: |
1989
|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00493848_v54_n3_p237_Monge http://hdl.handle.net/20.500.12110/paper_00493848_v54_n3_p237_Monge |
| Aporte de: |
| id |
paper:paper_00493848_v54_n3_p237_Monge |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_00493848_v54_n3_p237_Monge2023-06-08T15:05:49Z Heparin and Concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity Recondo, Eduardo Francisco calcium concanavalin a heparin magnesium anticoagulation methodology model nonbiological model nonhuman priority journal Binding, Competitive Blood Coagulation Calcium Concanavalin A Drug Interactions Heparin Kinetics Light Manganese Models, Biological Protein Conformation Scattering, Radiation Spectrophotometry Support, Non-U.S. Gov't A systematic study of the role of the Ca2+ and Mn2+ ions on the interaction between heparin and Concanavalin A was carried out. The protein was demetallized, and complex formation was followed by a light scattering assay. In the absence of ions no visible interaction was detected. Maximum activity was obtained when Mn2+ ions were added. A similar effect was observed when Ca2+ ions alone were used. Kinetics of the interaction in the presence of optimal Mn2+ and (or) Ca2+ concentrations confirmed the role of Ca2+ in accelerating a conformational change leading to a functional protein. A peculiar effect of activation-inhibition depending on ion concentration was also exhibited by Ca2+. These results confirm that Ca2+ and Mn2+ can occupy both sites on Concanavalin A and activate the protein for binding heparin. They point also to a crucial role of Ca2+ in the binding capacity of the active heparin fraction. Fil:Recondo, E.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1989 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00493848_v54_n3_p237_Monge http://hdl.handle.net/20.500.12110/paper_00493848_v54_n3_p237_Monge |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
calcium concanavalin a heparin magnesium anticoagulation methodology model nonbiological model nonhuman priority journal Binding, Competitive Blood Coagulation Calcium Concanavalin A Drug Interactions Heparin Kinetics Light Manganese Models, Biological Protein Conformation Scattering, Radiation Spectrophotometry Support, Non-U.S. Gov't |
| spellingShingle |
calcium concanavalin a heparin magnesium anticoagulation methodology model nonbiological model nonhuman priority journal Binding, Competitive Blood Coagulation Calcium Concanavalin A Drug Interactions Heparin Kinetics Light Manganese Models, Biological Protein Conformation Scattering, Radiation Spectrophotometry Support, Non-U.S. Gov't Recondo, Eduardo Francisco Heparin and Concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity |
| topic_facet |
calcium concanavalin a heparin magnesium anticoagulation methodology model nonbiological model nonhuman priority journal Binding, Competitive Blood Coagulation Calcium Concanavalin A Drug Interactions Heparin Kinetics Light Manganese Models, Biological Protein Conformation Scattering, Radiation Spectrophotometry Support, Non-U.S. Gov't |
| description |
A systematic study of the role of the Ca2+ and Mn2+ ions on the interaction between heparin and Concanavalin A was carried out. The protein was demetallized, and complex formation was followed by a light scattering assay. In the absence of ions no visible interaction was detected. Maximum activity was obtained when Mn2+ ions were added. A similar effect was observed when Ca2+ ions alone were used. Kinetics of the interaction in the presence of optimal Mn2+ and (or) Ca2+ concentrations confirmed the role of Ca2+ in accelerating a conformational change leading to a functional protein. A peculiar effect of activation-inhibition depending on ion concentration was also exhibited by Ca2+. These results confirm that Ca2+ and Mn2+ can occupy both sites on Concanavalin A and activate the protein for binding heparin. They point also to a crucial role of Ca2+ in the binding capacity of the active heparin fraction. |
| author |
Recondo, Eduardo Francisco |
| author_facet |
Recondo, Eduardo Francisco |
| author_sort |
Recondo, Eduardo Francisco |
| title |
Heparin and Concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity |
| title_short |
Heparin and Concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity |
| title_full |
Heparin and Concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity |
| title_fullStr |
Heparin and Concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity |
| title_full_unstemmed |
Heparin and Concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity |
| title_sort |
heparin and concanavalin a interaction as a model for studying the mechanism of the anticoagulant activity |
| publishDate |
1989 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00493848_v54_n3_p237_Monge http://hdl.handle.net/20.500.12110/paper_00493848_v54_n3_p237_Monge |
| work_keys_str_mv |
AT recondoeduardofrancisco heparinandconcanavalinainteractionasamodelforstudyingthemechanismoftheanticoagulantactivity |
| _version_ |
1768543027256623104 |