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

Enzyme Kinetics01:19

Enzyme Kinetics

Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...
Introduction to Enzyme Kinetics01:19

Introduction to Enzyme Kinetics

Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
Enzyme-Linked Immunosorbent Assay01:33

Enzyme-Linked Immunosorbent Assay

In 1971, Peter Perlman and Eva Engvall developed an Enzyme-linked immunosorbent assay (ELISA or EIA). ELISA differs from western blot in that the assays are conducted in microtiter plates or in vivo rather than on an absorbent membrane.
There are many different types of ELISAs, but they all involve an antibody molecule whose constant region binds an enzyme, leaving the variable region free to bind its specific antigen.  Enzyme-substrate reaction allows the antigen to be visualized or quantified.
Estimation of k and VD of Aminoglycosides01:20

Estimation of k and VD of Aminoglycosides

Aminoglycosides are a class of antibiotics used to treat various bacterial infections. Clinicians must determine the elimination rate constant (k) and volume of distribution (VD) to optimize therapeutic efficacy and minimize toxicity. The k value represents the rate at which the drug is removed from the body, and the VD reflects the degree to which the drug distributes into body tissues. Accurately estimating these parameters allows healthcare professionals to tailor drug dosing to individual...
Enzyme Inhibition01:30

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
Determination of Michaelis Constant and Maximum Elimination Rate01:20

Determination of Michaelis Constant and Maximum Elimination Rate

The Michaelis constant (KM) and the theoretical maximum process rate (Vmax) are vital parameters in the Michaelis-Menten equation, central to many biochemical reactions. They provide essential insights into enzyme kinetics and drug metabolism.
These parameters can be estimated by analyzing plasma concentration data post-drug administration. A notable example of this application is phenytoin, a drug with capacity-limited kinetics. It's recommended that phenytoin should be administered at two...

You might also read

Related Articles

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

Sort by
Same author

Quantitative proteomic profiling in brain subregions of mice exposed to open-field low-intensity blast reveals position-dependent blast effects.

Shock waves·2026
Same author

Cancer Decedents' Hospital End-of-Life Care Documentation: A Retrospective Review of Patient Records.

Journal of palliative care·2023
Same author

Experimental testing of a prototype cantilevered liquid-nitrogen-cooled silicon mirror.

Journal of synchrotron radiation·2023
Same author

Magnetic properties of γ-Fe<sub>2</sub>O<sub>3</sub> nanoparticles in a porous SiO<sub>2</sub> shell for drug delivery.

Journal of physics. Condensed matter : an Institute of Physics journal·2020
Same author

Size-dependent magnetic properties of γ-Fe<sub>2</sub>O<sub>3</sub> nanocrystallites.

Journal of physics. Condensed matter : an Institute of Physics journal·2019
Same author

Quality of Canned Celery Produced from Sliced Celery Stored Under Modified Atmospheres.

Journal of food protection·2019

Related Experiment Video

Updated: Jun 19, 2026

Qualitative and Quantitative Assays for Detection and Characterization of Protein Antimicrobials
10:50

Qualitative and Quantitative Assays for Detection and Characterization of Protein Antimicrobials

Published on: April 10, 2016

A VISCOSIMETRIC METHOD OF ESTIMATING ENZYME CONCENTRATION WITH SPECIAL REFERENCE TO AMYLASE.

W R Thompson1, C E Johnson, R Hussey

  • 1Department of Pathology, Yale University, New Haven.

The Journal of General Physiology
|October 30, 2009
PubMed
Summary
This summary is machine-generated.

Technical modifications to viscosimetric methods improve accuracy for enzyme concentration estimation. These refined techniques have been successfully used in irradiation studies for several years.

More Related Videos

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
13:00

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis
04:30

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis

Published on: January 17, 2025

Related Experiment Videos

Last Updated: Jun 19, 2026

Qualitative and Quantitative Assays for Detection and Characterization of Protein Antimicrobials
10:50

Qualitative and Quantitative Assays for Detection and Characterization of Protein Antimicrobials

Published on: April 10, 2016

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
13:00

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis
04:30

Quantifying the Modulation of Elastase Enzyme Activity Through Colorimetric Analysis

Published on: January 17, 2025

Area of Science:

  • Biochemistry
  • Physical Chemistry

Background:

  • Viscosimetric methods are crucial for studying enzyme kinetics.
  • Previous methods by Northrop and Hussey required technical refinement.

Purpose of the Study:

  • To present technical modifications of established viscosimetric methods.
  • To apply these improved methods for amylase concentration estimation.

Main Methods:

  • Detailed technical modifications to viscosimetric procedures.
  • Application of modified methods in multi-year irradiation studies.
  • Development of a novel amylase concentration estimation technique.

Main Results:

  • Satisfactory results were obtained using the modified viscosimetric techniques.
  • The refined methods proved effective in long-term irradiation studies.
  • Successful application to amylase concentration estimation.

Conclusions:

  • The presented technical modifications enhance viscosimetric method reliability.
  • These improvements facilitate accurate enzyme concentration determination.
  • The study validates the utility of refined viscosimetry in biochemical research.