A rapid method of oxymyoglobin purification
Related Experiment Video
Updated: May 27, 2026

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
Published on: October 3, 2018
P Gatellier1, M Anton, M Renerre
1INRA Theix, Station de Recherches sur la Viande, 63122, Saint-Genès Champanelle, France.
Abstract:
Oxymyoglobin was isolated from bovine Longissimus lumborum muscle by precipitation with ammonium sulfate and purification in rapid conditions with only one chromatographic step on Mono-Q HR column with a HPLC system. Purity of oxymyoglobin was controlled by SDS-polyacrylamide gel electrophoresis and isoelectrofocusing.
More Related Videos
09:24Synthesis, Hemoglobin Encapsulation and Biorthogonal PEGylation in Hierarchically Porous UiO-66 Nanoparticles for Oxygen Delivery Applications
Published on: May 8, 2026
10:14Expression and Purification of Nuclease-Free Oxygen Scavenger Protocatechuate 3,4-Dioxygenase
Published on: November 8, 2019