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...

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Autores principales: Monge, J.C., Recondo, E.F., Fernandez de Recondo, M.E.
Formato: JOUR
Lenguaje:English
Materias:
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
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00493848_v54_n3_p237_Monge
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id todo:paper_00493848_v54_n3_p237_Monge
record_format dspace
spelling todo:paper_00493848_v54_n3_p237_Monge2023-10-03T14:52:41Z Heparin and Concanavalin A interaction as a model for studying the mechanism of the anticoagulant activity Monge, J.C. Recondo, E.F. Fernandez de Recondo, M.E. 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. JOUR English info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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)
language English
orig_language_str_mv English
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
Monge, J.C.
Recondo, E.F.
Fernandez de Recondo, M.E.
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.
format JOUR
author Monge, J.C.
Recondo, E.F.
Fernandez de Recondo, M.E.
author_facet Monge, J.C.
Recondo, E.F.
Fernandez de Recondo, M.E.
author_sort Monge, J.C.
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
url http://hdl.handle.net/20.500.12110/paper_00493848_v54_n3_p237_Monge
work_keys_str_mv AT mongejc heparinandconcanavalinainteractionasamodelforstudyingthemechanismoftheanticoagulantactivity
AT recondoef heparinandconcanavalinainteractionasamodelforstudyingthemechanismoftheanticoagulantactivity
AT fernandezderecondome heparinandconcanavalinainteractionasamodelforstudyingthemechanismoftheanticoagulantactivity
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