Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
Sulfur Assimilation01:20

Sulfur Assimilation

Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to become...
Anticoagulant Drugs: Low-Molecular-Weight Heparins01:30

Anticoagulant Drugs: Low-Molecular-Weight Heparins

Hemostasis is a crucial process that prevents excessive blood loss from damaged blood vessels. It involves various mechanisms such as vasoconstriction, platelet adhesion and activation, and fibrin formation. The importance of each mechanism depends on the type of vessel injury. In contrast, thrombosis is the abnormal formation of a blood clot within the blood vessels, leading to potential complications if the clot obstructs blood flow. Thrombosis can be caused by increased coagulability of the...
Clot Retraction and Fibrinolysis01:16

Clot Retraction and Fibrinolysis

After a fibrin clot is formed, the next step is clot retraction, a vital process facilitated by platelet contractile proteins, such as actin and myosin. These proteins pull the fibrin strands closer together and condense the clot. This action reduces the size of the clot, creating a smaller, denser structure that effectively seals off the damaged vessel. Clot retraction consolidates the clot and helps with wound healing by bringing the edges of the damaged blood vessel closer together.
Extrinsic and Intrinsic Pathways of Hemostasis01:20

Extrinsic and Intrinsic Pathways of Hemostasis

Blood clotting or coagulation involves extrinsic and intrinsic pathways, which ultimately merge into the common pathway, forming a fibrin clot.
The Extrinsic Pathway
The extrinsic pathway of coagulation is typically initiated by tissue damage that exposes blood to tissue factor (TF), a protein released by the damaged tissue cells outside the blood vessels—this interaction with TF triggers biochemical reactions involving specific clotting factors. The key player here is Factor VII, which forms a...
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Prothrombotic fibrin clot phenotype in obstetric antiphospholipid syndrome: clinical implications and unanswered questions. Authors' reply.

Polish archives of internal medicine·2026
Same author

A review of the genetics and clinical manifestations of Donnai-Barrow syndrome.

Ophthalmic genetics·2026
Same author

Optic disc edema associated with neuroborreliosis.

IDCases·2025
Same author

Short-term performance of Symvess (acellular tissue engineered vessel-tyod) compared to external control data for autologous vein in treatment of extremity arterial injury.

Trauma surgery & acute care open·2025
Same author

Altered fibrin clot properties and the risk of thromboembolism in women with obstetric antiphospholipid syndrome: a cohort study.

Polish archives of internal medicine·2025
Same author

Beyond prothrombin time and activated partial thromboplastin time: coagulation in vivo-an illustrated review.

Laboratory medicine·2025
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

Related Experiment Video

Updated: May 13, 2026

Extracellular Vesicle Tissue Factor Activity Assay
03:53

Extracellular Vesicle Tissue Factor Activity Assay

Published on: December 29, 2023

Disulfide reduction abolishes tissue factor cofactor function.

Jolanta Krudysz-Amblo1, Mark E Jennings, Tyler Knight

  • 1Department of Biochemistry, University of Vermont, Colchester, VT 05446, USA.

Biochimica Et Biophysica Acta
|February 26, 2013
PubMed
Summary
This summary is machine-generated.

Disulfide bonds in tissue factor (TF) are crucial for its blood coagulation activity. Reducing these bonds abolishes TF

More Related Videos

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Flow Cytometry Analysis of Tissue Factor Expression in Human Platelets
10:08

Flow Cytometry Analysis of Tissue Factor Expression in Human Platelets

Published on: November 22, 2024

Related Experiment Videos

Last Updated: May 13, 2026

Extracellular Vesicle Tissue Factor Activity Assay
03:53

Extracellular Vesicle Tissue Factor Activity Assay

Published on: December 29, 2023

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture
09:37

Combining Non-reducing SDS-PAGE Analysis and Chemical Crosslinking to Detect Multimeric Complexes Stabilized by Disulfide Linkages in Mammalian Cells in Culture

Published on: May 2, 2019

Flow Cytometry Analysis of Tissue Factor Expression in Human Platelets
10:08

Flow Cytometry Analysis of Tissue Factor Expression in Human Platelets

Published on: November 22, 2024

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Hematology

Background:

  • Tissue factor (TF) initiates blood coagulation and is a transmembrane protein.
  • A debate exists regarding the role of specific disulfide bonds (Cys186-Cys209) in TF's procoagulant function.
  • Previous studies relied on indirect evidence from oxidizing/reducing reagents.

Purpose of the Study:

  • To directly determine the disulfide status of TF.
  • To investigate the functional consequences of TF disulfide reduction.

Main Methods:

  • Mass spectrometry was used to analyze disulfide bonds in native and reduced recombinant and placental TF.
  • Functional assays assessed TF's cofactor activity.

Main Results:

  • All four extracellular cysteines in native TF are oxidized.
  • Reduced TF binds factor VIIa but loses all cofactor function.
  • Disulfide reduction eliminates TF's regulation of factor VIIa catalytic function.

Conclusions:

  • TF disulfide integrity is essential for its procoagulant cofactor activity.
  • This study clarifies TF structure-function relationships.
  • Findings provide direct evidence on TF's regulatory mechanism in coagulation.