• Journal of the Korean Wood Science and Technology
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• v.29 no.4
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• pp.79-88
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• 2001

Lectin was isolated from shiitake mushroom (Lentinula edodes) with 0.15 M NaCl solution, and purified by the following procedures : precipitation by ammonium sulfate, anion exchange column chromatography on DEAE Sephadex A-50 and hydroxyapatite column chromatography. The fresh pileus part of the mushroom contained more than two times of lectin compared to the stipe part, and lectins and its activity were reduced by heating. The extraction yield of crude lectin was 46.03%, 28% yield after purification on on DEAE Sephadex A-50 column chromatography. Some amino acids, aspartic acid, serine, alanine and histidine, were increased by purification process. Relatively low molecular weight parts of lectin had the agglutinating activity for rabbit blood, and its molecular weight was about 23 kDa The molecular weights of purified lectins, LA-a and LB-b, by the hydroxyapatite column chromatography were 24 kDa and 23 kDa, respectively.