The active fraction of heparin enclose both properties: Anticoagulant and anticomplement
Heparin binds antithrombin and increases more than thousand times the rate of the anticoagulant activity. Another activity of heparin is the inhibition of the human complement system. The results from several laboratories have shown that both biological activities of heparin are independent. The mai...
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todo:paper_03252957_v37_n2_p193_Recondo2023-10-03T15:23:35Z The active fraction of heparin enclose both properties: Anticoagulant and anticomplement Recondo, E.F. Calabrese, G. Fernández, M.E. Calcium ions First component of the complement system Heparin Low ionic strength Molecular interactions anticoagulant agent calcium ion complement inhibitor concanavalin A heparin anticoagulation article complement inhibition complement system controlled study human ionic strength molecular interaction precipitation Heparin binds antithrombin and increases more than thousand times the rate of the anticoagulant activity. Another activity of heparin is the inhibition of the human complement system. The results from several laboratories have shown that both biological activities of heparin are independent. The main aim of this work was to study how heparin and antithrombin recognize each other. First experiments were done with the system heparin and Concanavalin A. The lectin recognizes and precipitates the fraction of the heparin molecule with high affinity for antithrombin, and high anticoagulant activity. Low ionic strength and the presence of calcium ions are absolute requirements for the recognition. When, instead of Con A, the first component of the complement system was used for the interaction, and under similar and very specific conditions, again precipitate the fraction of heparin with high affinity for antithrombin and high anticoagulant activity. The conclusion is that both heparin biological activities reside in the same limited fraction of the molecule which containes the segment with high affinity for antitrombin. These results are in opposition with most reported in the literature, but we have demonstrated that specific interactions between macromolecules only detect it under very low ionic strength, and in the presence of calcium ions. Fil:Recondo, E.F. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03252957_v37_n2_p193_Recondo |
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 ions First component of the complement system Heparin Low ionic strength Molecular interactions anticoagulant agent calcium ion complement inhibitor concanavalin A heparin anticoagulation article complement inhibition complement system controlled study human ionic strength molecular interaction precipitation |
spellingShingle |
Calcium ions First component of the complement system Heparin Low ionic strength Molecular interactions anticoagulant agent calcium ion complement inhibitor concanavalin A heparin anticoagulation article complement inhibition complement system controlled study human ionic strength molecular interaction precipitation Recondo, E.F. Calabrese, G. Fernández, M.E. The active fraction of heparin enclose both properties: Anticoagulant and anticomplement |
topic_facet |
Calcium ions First component of the complement system Heparin Low ionic strength Molecular interactions anticoagulant agent calcium ion complement inhibitor concanavalin A heparin anticoagulation article complement inhibition complement system controlled study human ionic strength molecular interaction precipitation |
description |
Heparin binds antithrombin and increases more than thousand times the rate of the anticoagulant activity. Another activity of heparin is the inhibition of the human complement system. The results from several laboratories have shown that both biological activities of heparin are independent. The main aim of this work was to study how heparin and antithrombin recognize each other. First experiments were done with the system heparin and Concanavalin A. The lectin recognizes and precipitates the fraction of the heparin molecule with high affinity for antithrombin, and high anticoagulant activity. Low ionic strength and the presence of calcium ions are absolute requirements for the recognition. When, instead of Con A, the first component of the complement system was used for the interaction, and under similar and very specific conditions, again precipitate the fraction of heparin with high affinity for antithrombin and high anticoagulant activity. The conclusion is that both heparin biological activities reside in the same limited fraction of the molecule which containes the segment with high affinity for antitrombin. These results are in opposition with most reported in the literature, but we have demonstrated that specific interactions between macromolecules only detect it under very low ionic strength, and in the presence of calcium ions. |
format |
JOUR |
author |
Recondo, E.F. Calabrese, G. Fernández, M.E. |
author_facet |
Recondo, E.F. Calabrese, G. Fernández, M.E. |
author_sort |
Recondo, E.F. |
title |
The active fraction of heparin enclose both properties: Anticoagulant and anticomplement |
title_short |
The active fraction of heparin enclose both properties: Anticoagulant and anticomplement |
title_full |
The active fraction of heparin enclose both properties: Anticoagulant and anticomplement |
title_fullStr |
The active fraction of heparin enclose both properties: Anticoagulant and anticomplement |
title_full_unstemmed |
The active fraction of heparin enclose both properties: Anticoagulant and anticomplement |
title_sort |
active fraction of heparin enclose both properties: anticoagulant and anticomplement |
url |
http://hdl.handle.net/20.500.12110/paper_03252957_v37_n2_p193_Recondo |
work_keys_str_mv |
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1782030336907018240 |