Related Experiment Video
Updated: Aug 8, 2026

Capillary Electrophoresis-based Hydrogen/Deuterium Exchange for Conformational Characterization of Proteins with Top-down Mass Spectrometry
Published on: June 8, 2021
Microheterogeneity of globulin-1 storage protein from French bean with isoelectrofocusing
J W Brown1, F A Bliss, T C Hall
1Department of Horticulture, University of Wisconsin, Madison, Wisconsin 53706.
Abstract:
The major storage protein fraction, globulin-1 protein, of French bean (Phaseolus vulgaris L.) was analyzed by two-dimensional electrophoresis. The protein pattern suggested a more complex system for globulin-1 protein than the model of three polypeptides, alpha, beta, and gamma, differing in molecular weight. Isoelectrofocusing analyses of the individual proteins showed that each exhibited charge microheterogeneity over a similar pH range. Isoelectrofocusing banding patterns may help to understand the relationships between the globulin-1 polypeptide subunits.
More Related Videos
14:44A Protocol for the Identification of Protein-protein Interactions Based on 15N Metabolic Labeling, Immunoprecipitation, Quantitative Mass Spectrometry and Affinity Modulation
Published on: September 24, 2012
08:31Total Protein Extraction and 2-D Gel Electrophoresis Methods for Burkholderia Species
Published on: October 15, 2013
Related Concept Videos
Two-dimensional Gel Electrophoresis
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as cells...
SDS-PAGE
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...