Related Experiment Video
Updated: May 1, 2026
Identification of Protein Interacting Partners Using Tandem Affinity Purification
Published on: February 25, 2012
Isolation, purification & properties of lactose binding agglutination factor from rabbit skeletal muscle
Abstract:
The lactose binding agglutination factor from rabbit skeletal muscle is isolated through the use of lactose and urea. The factor is purified with DEAE cellulose and Sepharose 4B chromatography. The molecular weight of the factor is determined with Sephadex G-75 chromatography and found to be 28,000 Daltons. The subunit's molecular weight is determined by SDS gel electrophoresis, and found to be 14,000 Daltons. It was found that this binding factor can agglutinate trypsin-treated rabbit erythrocytes. Moreover, this agglutination is inhibited by EDTA and lactose.
More Related Videos
10:33Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow
Published on: January 8, 2014
05:58Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
Published on: February 24, 2026