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

Antihypertensive Drugs: Direct Renin Inhibitors01:25

Antihypertensive Drugs: Direct Renin Inhibitors

The renin-angiotensin-aldosterone system (RAAS) is an intricate physiological pathway involving numerous enzymes and hormones, including renin, angiotensin-converting enzyme (ACE), angiotensin I and II, and aldosterone. Imbalances within this system increase the production of angiotensin II and aldosterone. Increased angiotensin II levels promote vasoconstriction and blood pressure elevation. Concurrently, higher aldosterone levels stimulate sodium and water reabsorption in the kidneys,...
Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors01:30

Antihypertensive Drugs: Angiotensin-Converting Enzyme Inhibitors

Angiotensin-converting enzyme (ACE), a vital component of the renin-angiotensin-aldosterone system, is abundant in lung endothelial cells. ACE converts the inactive decapeptide, angiotensin I, into the active octapeptide, angiotensin II. This potent vasoconstrictor narrows blood vessels, increasing resistance to blood flow and elevating blood pressure. Angiotensin II also stimulates aldosterone production, encouraging kidney cells to reabsorb more sodium and water from urine, thereby increasing...
Inhibitors of Bacterial Protein Synthesis01:25

Inhibitors of Bacterial Protein Synthesis

Aminoglycosides constitute a highly potent class of bactericidal antibiotics that exert their antimicrobial effects by targeting the bacterial ribosome, specifically disrupting protein synthesis. These polycationic molecules consist of amino-modified sugars linked via glycosidic bonds to an aminocyclitol core such as 2-deoxystreptamine or streptamine. Their strong positive charges facilitate tight binding to the negatively charged phosphate backbone of ribosomal RNA (rRNA), primarily at the 16S...
Indirect-Acting Cholinergic Agonists: Mechanism of Action01:18

Indirect-Acting Cholinergic Agonists: Mechanism of Action

Indirect-acting cholinergic agonists work by interacting with an enzyme called acetylcholinesterase (AChE) in the synaptic cleft. They can be reversible or irreversible inhibitors and have different effects on the enzyme.
Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex, leading to...
Inhibitors of Viral Protein Synthesis01:30

Inhibitors of Viral Protein Synthesis

Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...
Antihypertensive Drugs: Angiotensin II Receptor Blockers01:30

Antihypertensive Drugs: Angiotensin II Receptor Blockers

In the renin-angiotensin-aldosterone system, a hormone called angiotensin II plays a crucial role. It binds to the AT1 receptors in vascular smooth muscles coupled with Gq proteins. The activation of these receptors activates an enzyme called phospholipase C, which releases two molecules: inositol trisphosphate and diacylglycerol. These molecules cause a chain reaction that leads to the phosphorylation of myosin light chains and promotes interaction between actin and myosin, leading to smooth...

You might also read

Related Articles

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

Sort by
Same author

Diagnostic ultrasound activates pure prekallikrein.

Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis·2012
Same author

Determination of the anti-F10a or anti-F2a generation action of rivaroxaban or dabigatran.

Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis·2012
Same author

Bilirubin and microangiopathy.

Ophthalmology·2012
Same author

The ultrasound frequency determines the degree of intrinsic coagulation activation.

Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis·2012
Same author

Lamotrigine triggers the contact phase of coagulation.

Epileptic disorders : international epilepsy journal with videotape·2012
Same author

Contact activation of coagulation depends on the maximal lipophilic trigger concentration.

Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis·2012

Related Experiment Video

Updated: Jul 15, 2026

Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus
06:45

Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus

Published on: June 2, 2023

Arginine inhibits serpins.

Thomas W Stief1

  • 1Department of Clinical Chemistry, University Hospital, Giessen/Marburg, Germany, thstief@med.uni-marburg.de

Clinical and Applied Thrombosis/Hemostasis : Official Journal of the International Academy of Clinical and Applied Thrombosis/Hemostasis
|April 26, 2007
PubMed
Summary

High concentrations of arginine effectively inhibit serine protease inactivators (serpins), crucial for stabilizing biological samples. This finding offers a novel method for inhibiting pathogens reliant on serpins.

Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • Serine protease inactivators (serpins) are key regulators in biological systems.
  • Stabilizing biological samples often requires inhibiting serpin activity.
  • Arginine's guanidine group interacts with the active sites of serine proteases.

Purpose of the Study:

  • To investigate the inhibitory effect of arginine on serpins.
  • To determine the concentration of arginine required to inhibit serpin activity.
  • To explore potential applications of arginine as an inhibitor in biological stabilization and pathogen control.

Main Methods:

  • Assays were performed using pooled normal plasma or human albumin.
  • Reactions involved varying concentrations of arginine (0-2.67 M) at pH 8.6.

More Related Videos

Induction of Nephrotic Syndrome in Mice by Retrobulbar Injection of Doxorubicin and Prevention of Volume Retention by Sustained Release Aprotinin
07:38

Induction of Nephrotic Syndrome in Mice by Retrobulbar Injection of Doxorubicin and Prevention of Volume Retention by Sustained Release Aprotinin

Published on: May 6, 2018

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

Related Experiment Videos

Last Updated: Jul 15, 2026

Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus
06:45

Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus

Published on: June 2, 2023

Induction of Nephrotic Syndrome in Mice by Retrobulbar Injection of Doxorubicin and Prevention of Volume Retention by Sustained Release Aprotinin
07:38

Induction of Nephrotic Syndrome in Mice by Retrobulbar Injection of Doxorubicin and Prevention of Volume Retention by Sustained Release Aprotinin

Published on: May 6, 2018

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

  • Enzyme activities (thrombin, plasmin, C1-esterase) were measured using chromogenic substrates and a microtiter plate reader.

    • Main Results:

    • Arginine inhibited plasmatic antithrombin activity with an IC(50) of 580 mM.
    • Arginine inhibited plasmatic alpha(2)-antiplasmin and C1-inactivator with an IC(25) of 1650 mM.
    • Arginine demonstrated similar IC(50) values (around 400 mM) against the amidolytic activity of thrombin, plasmin, and C1-esterase.

    Conclusions:

    • Very high concentrations of arginine inhibit serpins, aiding in biological sample stabilization.
    • Arginine's inhibitory effect on serpins presents a potential gentle method for pathogen inhibition.
    • This research highlights arginine's dual role in inhibiting both serine proteases and serpins at high concentrations.