It was also found to be thermally stable from 0 deg C to 60 deg C. It was found to be stable at pH 2 to pH 10. The native lectin has an estimated molecular weight of 640 KD composed of six sub-units with the following molecular weights: 140, 130, 120, 95, 90 and 85 KD.

Hapten inhibition of agglutination did not show specificity towards any of the sugar standards tested. Trypsinization has a positive effect on the agglutination behavior of the crude protein. The lectin is also classified as a complete type since it agglutinated untreated erythrocytes. The lectin is non blood type and non blood group specific since it agglutinated human erythrocytes of all human blood types (A, B, O and AB) as well as animal erythrocytes (calf). Total sugars and identification of the sugar components were also determined by the phenol-sulfuric acid method and HPLC, respectively. Factors that could possibly affect lectin activity like pH and temperature, were also evaluated.

Agglutination using blood types A, B, O and AB was used to assay the presence of lectin. The sugar residues were identified by HPLC analysis as melibiose and probably other oligosaccharidesДЄ lectin was isolated from the wood ear fungus (Auricularia auricula) by protein extraction using phosphate buffered saline (PBS) pH 7.2, ammonium sulfate fractionation and gel permeation chromatography using Sephadex G-200. It is a glycoprotein containing 3.15 percent total sugar. A lectin was isolated from the wood ear fungus (Auricularia auricula) by protein extraction using phosphate buffered saline (PBS) pH 7.2, ammonium sulfate fractionation and gel permeation chromatography using Sephadex G-200.

Auricularia auricula underw recipe