Marasmium Oreades Lectin Production Service
The Marasmius oreades mushroom lectin (MOA) is a type B erythrocyte agglutinin. MOA is a 50 kDa heterodimeric protein with subunits 33 and 23 kDa, respectively. MOA specifically recognizes structures containing Gal 1,3- and shows the highest affinity for the branching blood group B triose Gal 1,3 (Fuc 1,2) Gal. But with no affinity for the isomers 1,2-, 1,4-, and 1,6-disaccharides. MOA has two carbohydrate-binding domains, the N- and C-terminal domains. In addition, MOA has an enzymatic catalytic activity.
MOA Extraction and Purification Service at CD BioGlyco
Collect the Marasmius oreades mushroom in a natural environment. Clean up the soil and cut it into small pieces. Fresh mushroom pieces are added to the buffer. When the mixture is stirred for a few minutes at a low temperature, filter it. The supernatant is mixed with solid ammonium sulfate. The precipitation is removed by centrifugation. Solid ammonium sulfate is added to the supernatant again and stirred overnight. Collecting the precipitated fraction, adding a buffer to dissolve, then dialysis. Fractions are first purified using an agarose gel column and eluted under absorbance monitoring. Second, the collected fractions are treated and purified using an affinity chromatography column. The bound lectins are eluted using the configured buffer. Collect the target components.
Fig.1 Flow chart of extraction and separation of MOA. (CD BioGlyco)
MOA Analysis Service at CD BioGlyco
For purified Fungal Lectins, it is important to understand all aspects to better develop their functional properties. Notably, our company offers a wide range of products and services related to MOA. Combining multiple glycobiology platforms, we provide fast and accurate analytical services:
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Research Literature Based on MOA
Paper Title: Marasmius oreades agglutinin (MOA) is a chimerolectin with proteolytic activity
Journal: Biochemical and Biophysical Research Communications
IF: 3.575
Published: 2011
Results: The 1-antitrypsin treatment with MOA in the presence of calcium resulted in a single band, shifted towards the lower molecular weight. Meanwhile, MOA proteolytic activity was highly correlated with the presence of divalent cations, especially for calcium and manganese. In the absence of both metal ions, no activity was observed. The addition of metal ions did not act as a substitute for calcium or manganese. The structure of the glycan was not altered by mass spectrometry, thus indicating that MOA did not exhibit N-glycanase activity.
Fig.2 Schematic diagram of substrate bands tested by SDS-PAGE analysis. (Cordara, et al., 2011)
Applications of MOA
- MOA is the major component of the anti-NF-κB activity in the Marasmius oreades mushroom.
- MOA inhibits the growth and development of nematodes and amoebae through a specific carbohydrate-binding capacity.
- MOA plays a great role in protecting mushroom-fruiting bodies from flapping eaters.
Advantages of Us
- The separation and purification services we provide avoid the effects of proteolysis and oxidation and ensure high-quality services.
- Our company has a well-trained technical team and advanced equipment, which customize services according to client needs.
CD BioGlyco has many years of service experience in Lectin Production. We are recognized by our clients in various countries for our attentive service and high-quality products. Please feel free to contact us if you want to know more.
References
- Winter, H.C.; et al. The mushroom Marasmius oreades lectin is a blood group type B agglutinin that recognizes the Galα1, 3Gal and Galα1, 3Galβ1, 4GlcNAc porcine xenotransplantation epitopes with high affinity. J Biol Chem. 2002, 277(17): 14996-5001.
- Kruger, R.P.; et al. Cloning, expression, and characterization of the Galα 1,3Gal high affinity lectin from the mushroom Marasmius oreades. J Biol Chem. 2002, 277(17): 15002-5.
- Cordara, G.; et al. Marasmius oreades agglutinin (MOA) is a chimerolectin with proteolytic activity. Biochem Biophys Res Commun. 2011, 408(3): 405-10.
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