Related Experiment Video
Updated: Aug 17, 2026
Purification of the M. magneticum Strain AMB-1 Magnetosome Associated Protein MamAΔ41
Published on: March 25, 2010
[Purification and separation of mannan-binding lectin (MBL) and MBL-associated serine proteases complex from human
Yue Chen1, Li-yun Zhang, Zheng-liang Chen
1Department of Immunology, Southern Medical University, Guangzhou 510515, China. chenyue@fimmu.com
Objective:
To separate mannan-binding lectin (MBL) and MBL-associated serine proteases (MASPs) from human plasma.
Methods:
A two-step affinity chromatography on underivatized sepharose 4B was employed for purification of MBL-MASP complex, followed by gel filtration on a Sephacryl S-300 column for separation of MBL and MASPs from the complex. The purification procedures were performed at 4 degrees Celsius with the addition of two proteolytic inhibitors, phenyl methylsulfonyl fluoride and 1,10-phenanthroline during affinity chromatography but not in the gel filtration buffer.
Results:
Preparations of highly purified MBL and proenzyme MASPs were obtained. The purified MBL was shown by SDS-PAGE and Western blotting to be a functional multimer composed of 28,000 and 32,000 peptide chains, with high bioactivity as demonstrated by ligand-binding assay and yeast agglutination experiment.
Conclusion:
A simple and convenient procedure is established successfully for the purification of MBL and the proenzyme MASPs.
