Isolation of a novel N-acetylglucosamine-specific lectin from fresh sclerotia of the edible mushroom Pleurotus tuber-regium.
An N-acetylglucosamine-binding lectin with a molecular mass of 32kDa was isolated from fresh sclerotia of the edible mushroom Pleurotus tuber-regium. Its N-terminal sequence exhibited some similarity to that of Agaricus bisporus lectin. The isolation procedure was simple, involving (NH(4))(2)SO(4) precipitation, ion exchange chromatography on DEAE-cellulose, affinity chromatography on N-acetyl-D-glucosamine-agarose, and gel filtration by fast protein liquid chromatography on Superdex 75. The lectin exhibited hemagglutinating activity toward trypsinized rabbit erythrocytes but not toward untrypsinized rabbit erythrocytes.
Wang
Hexiang
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Department of Microbiology, College of Biological Science, China Agricultural University, Beijing, China.
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D000117:Acetylglucosamine / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D006386:Hemagglutination Tests; D037102:Lectins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*; D008969:Molecular Sequence Data; D020076:Pleurotus / Q000737:chemistry*; D011817:Rabbits; D020539:Sequence Analysis, Protein
C041433:Agaricus lectins; D005656:Fungal Proteins; D037102:Lectins; D000117:Acetylglucosamine