Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Enzyme-Linked Immunosorbent Assay

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.

Amperometry: Overview

Amperometry: Overview

Amperometry is a technique commonly used to measure the concentration of specific analytes in a solution by monitoring the electric current generated during an electrochemical reaction. It involves applying a constant potential between a working electrode and a reference electrode to measure the resulting current, which is proportional to the concentration of the analyte. The Clark oxygen electrode operates based on this principle of amperometry. It consists of a cathode and an anode enclosed...

Protein-Drug Binding: Determination Methods

Protein-Drug Binding: Determination Methods

Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...

You might also read

Related Articles

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

Sort by

Same journal

[On the potential protective properties of vitamin A in carcinogenesis].

Ukrains'kyi biokhimichnyi zhurnal·1977

Same journal

[Stimulation of gluconeogenesis with 1,3-butanediol in the perfused rat liver].

Ukrains'kyi biokhimichnyi zhurnal·1977

Same journal

[Isoenzymic spectra of lactate dehydrogenase and malate dehydrogenase in the loach unfertilized eggs and embryos].

Ukrains'kyi biokhimichnyi zhurnal·1977

Same journal

[Carboxypeptidases from different microbiolorganisms].

Ukrains'kyi biokhimichnyi zhurnal·1977

Same journal

[Intake dynamics of GABA and its pantoate derivative in mice brain areas].

Ukrains'kyi biokhimichnyi zhurnal·1977

Same journal

[Peculiarities of the action of protein positively reacting in the sedimentation test for cancer on the activity of glycolytic enzymes].

Ukrains'kyi biokhimichnyi zhurnal·1977

Search research articles

Related Experiment Video

Updated: Jun 29, 2026

Microvolume Protein Concentration Determination using the NanoDrop 2000c Spectrophotometer

Microvolume Protein Concentration Determination using the NanoDrop 2000c Spectrophotometer

Published on: November 5, 2009

Amperometric method for quantitative determination of proteins

E M Skobets', A P Megalins'ka

Ukrains'Kyi Biokhimichnyi Zhurnal

|November 1, 1977

Summary

A novel amperometric method offers accurate quantitative protein determination using copper complexation. This sensitive technique works at any pH and can even measure stained proteins, outperforming the Lawry method.

Area of Science:

Analytical Chemistry
Biochemistry

Background:

Accurate protein quantification is crucial in biochemical research.
Existing methods like the Lawry method have limitations in accuracy and pH dependency.

Purpose of the Study:

To introduce and validate a new amperometric method for quantitative protein determination.
To highlight the advantages of this novel technique over existing methods.

Main Methods:

Utilized an amperometric approach based on copper's ability to form intracomplex compounds with proteins.
Exploited the formation of insoluble compounds between copper-protein complexes and potassium ferrocyanide for detection.

Main Results:

Achieved a high sensitivity of 10 micrograms of protein per milliliter.

More Related Videos

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Highly Sensitive and Quantitative Detection of Proteins and Their Isoforms by Capillary Isoelectric Focusing Method

Highly Sensitive and Quantitative Detection of Proteins and Their Isoforms by Capillary Isoelectric Focusing Method

Published on: September 19, 2018

Related Experiment Videos

Last Updated: Jun 29, 2026

Microvolume Protein Concentration Determination using the NanoDrop 2000c Spectrophotometer

Microvolume Protein Concentration Determination using the NanoDrop 2000c Spectrophotometer

Published on: November 5, 2009

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Selected Reaction Monitoring Mass Spectrometry for Absolute Protein Quantification

Published on: August 17, 2015

Highly Sensitive and Quantitative Detection of Proteins and Their Isoforms by Capillary Isoelectric Focusing Method

Highly Sensitive and Quantitative Detection of Proteins and Their Isoforms by Capillary Isoelectric Focusing Method

Published on: September 19, 2018

Demonstrated superior accuracy (5%) compared to the Lawry method.

Confirmed the method's applicability across all pH ranges.

Showed successful determination of stained proteins.

Conclusions:

The described amperometric method provides a sensitive, accurate, and versatile alternative for protein quantification.
Its ability to function at any pH and with stained proteins offers significant advantages for various applications.