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.
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)
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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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)
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