What question did this study set out to answer?

To determine whether plasma-activated Factor X inhibitor, antithrombin III, and heparin cofactor represent separate entities or functions of a single blood proteinase inhibitor.

June 1, 1971Journal of Biological ChemistryOpen Access

Identity of Plasma-activated Factor X Inhibitor with Antithrombin III and Heparin Cofactor

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Authors

EYE.T. YinFirst People's Hospital of Chongqing SWStanford WesslerVascular / Pulmonary Vascular PSPamela J. StollJewish Hospital

Discussion

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Overview

Biochemical study demonstrates identity between Factor X inhibitor, antithrombin III, and heparin cofactor in plasma, indicating a unified proteinase inhibitor regulates blood clotting.

Key Points

To determine whether plasma-activated Factor X inhibitor, antithrombin III, and heparin cofactor represent separate entities or functions of a single blood proteinase inhibitor.
Purified the plasma inhibitor using Sephadex G-200, DEAE-Sephadex, and DEAE-cellulose chromatography, along with preparative polyacrylamide gel disc electrophoresis.
Evaluated functional cross-reactivity and physical characteristics via 56°C thermal inactivation assays, reciprocal neutralization with thrombin, and gel filtration under varying ionic strengths (0.01 M to 0.30 M NaCl) in the presence of heparin.
Antithrombin III, activated Factor X inhibitor, and heparin cofactor activities cochromatographed identically across all column matrices and comigrated during electrophoresis.
Heating to 56°C caused simultaneous inactivation of both antithrombin III and activated Factor X inhibitory activities, while complete neutralization with thrombin abolished Factor X inhibition and vice versa.
Gel filtration confirmed that the inhibitor binds heparin to elute as a single complex, demonstrating that all three anticoagulant activities reside within the same broad-specificity protein.

Cite This Study

Yin et al. (1971) studied this question.

synapsesocial.com/papers/6a8663eeae12ed54832fe2da https://doi.org/10.1016/s0021-9258(18)62185-4

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June 1, 1971Journal of Biological ChemistryOpen Access

Identity of Plasma-activated Factor X Inhibitor with Antithrombin III and Heparin Cofactor

View Full Paper

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Bookmark

Authors

EYE.T. YinFirst People's Hospital of Chongqing SWStanford WesslerVascular / Pulmonary Vascular PSPamela J. StollJewish Hospital

Discussion

Member takes

Overview

Biochemical study demonstrates identity between Factor X inhibitor, antithrombin III, and heparin cofactor in plasma, indicating a unified proteinase inhibitor regulates blood clotting.

Key Points

To determine whether plasma-activated Factor X inhibitor, antithrombin III, and heparin cofactor represent separate entities or functions of a single blood proteinase inhibitor.
Purified the plasma inhibitor using Sephadex G-200, DEAE-Sephadex, and DEAE-cellulose chromatography, along with preparative polyacrylamide gel disc electrophoresis.
Evaluated functional cross-reactivity and physical characteristics via 56°C thermal inactivation assays, reciprocal neutralization with thrombin, and gel filtration under varying ionic strengths (0.01 M to 0.30 M NaCl) in the presence of heparin.
Antithrombin III, activated Factor X inhibitor, and heparin cofactor activities cochromatographed identically across all column matrices and comigrated during electrophoresis.
Heating to 56°C caused simultaneous inactivation of both antithrombin III and activated Factor X inhibitory activities, while complete neutralization with thrombin abolished Factor X inhibition and vice versa.
Gel filtration confirmed that the inhibitor binds heparin to elute as a single complex, demonstrating that all three anticoagulant activities reside within the same broad-specificity protein.

Cite This Study

Yin et al. (1971) studied this question.

synapsesocial.com/papers/6a8663eeae12ed54832fe2da https://doi.org/10.1016/s0021-9258(18)62185-4

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