What question did this study set out to answer?

To determine whether sequence-specific antibodies directed against residues 62–73 of the human alpha-thrombin B-chain can identify and functionally characterize a secondary binding site.

August 1, 1988Journal of Biological ChemistryOpen Access

The use of sequence-specific antibodies to identify a secondary binding site in thrombin.

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Authors

GNG. NoéUniversität Ulm JHJan HofsteengeFriedrich Miescher Institute GRG RovelliItalfarmaco (Italy)

Discussion

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Overview

In vitro study reveals competitive inhibition of hirudin and fibrinogen binding by thrombin sequence-specific antibodies, demonstrating a critical secondary recognition exosite.

Key Points

To determine whether sequence-specific antibodies directed against residues 62–73 of the human alpha-thrombin B-chain can identify and functionally characterize a secondary binding site.
Synthesized a peptide corresponding to residues 62–73 of the human alpha-thrombin B-chain and generated polyclonal antibodies against it.
Assayed antibody interactions across small chromogenic substrate hydrolysis, antithrombin III inactivation, hirudin binding, fibrinogen cleavage, and thrombomodulin-dependent protein C activation.
Purified antibodies did not alter small-substrate hydrolysis and reduced the antithrombin III second-order inactivation rate constant by only 20%.
Antibodies competitively inhibited hirudin binding across 0–43 nM with a dissociation constant of 3.4 ± 0.5 nM, and inhibited fibrinopeptide A release from fibrinogen with an inhibition constant of 11.7 ± 0.4 nM.
Protein C activation in the presence of thrombomodulin was inhibited with an apparent inhibition constant of 10.7 ± 1.5 nM, whereas protein C activation without thrombomodulin remained unaffected.

Cite This Study

Noé et al. (1988) studied this question.

synapsesocial.com/papers/6a764df4329619356706dfd1 https://doi.org/10.1016/s0021-9258(18)37844-x

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August 1, 1988Journal of Biological ChemistryOpen Access

The use of sequence-specific antibodies to identify a secondary binding site in thrombin.

View Full Paper

Ask AI

Bookmark

Authors

GNG. NoéUniversität Ulm JHJan HofsteengeFriedrich Miescher Institute GRG RovelliItalfarmaco (Italy)

Discussion

Member takes

Overview

In vitro study reveals competitive inhibition of hirudin and fibrinogen binding by thrombin sequence-specific antibodies, demonstrating a critical secondary recognition exosite.

Key Points

To determine whether sequence-specific antibodies directed against residues 62–73 of the human alpha-thrombin B-chain can identify and functionally characterize a secondary binding site.
Synthesized a peptide corresponding to residues 62–73 of the human alpha-thrombin B-chain and generated polyclonal antibodies against it.
Assayed antibody interactions across small chromogenic substrate hydrolysis, antithrombin III inactivation, hirudin binding, fibrinogen cleavage, and thrombomodulin-dependent protein C activation.
Purified antibodies did not alter small-substrate hydrolysis and reduced the antithrombin III second-order inactivation rate constant by only 20%.
Antibodies competitively inhibited hirudin binding across 0–43 nM with a dissociation constant of 3.4 ± 0.5 nM, and inhibited fibrinopeptide A release from fibrinogen with an inhibition constant of 11.7 ± 0.4 nM.
Protein C activation in the presence of thrombomodulin was inhibited with an apparent inhibition constant of 10.7 ± 1.5 nM, whereas protein C activation without thrombomodulin remained unaffected.

Cite This Study

Noé et al. (1988) studied this question.

synapsesocial.com/papers/6a764df4329619356706dfd1 https://doi.org/10.1016/s0021-9258(18)37844-x

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