1. Purification and characterization of a lectin from the mushroom Hypsizigus marmoreus.
- Author
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Suzuki, Tomohiro, Abe, Tomoya, Umehara, Kanako, Choi, Jae-Hoon, Hirai, Hirofumi, Dohra, Hideo, and Kawagishi, Hirokazu
- Subjects
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LECTINS , *GLYCOPROTEINS , *SUBMANDIBULAR gland , *BLOOD agglutination , *HEMAGGLUTINATION tests , *GEL permeation chromatography - Abstract
HML ( Hypsizigus marmoreus lectin) was isolated from the mushroom Hypsizigus marmoreus using CM cation exchange, bovine submaxillary gland mucin affinity column and TSK-GEL G3000SW gel filtration chromatography. The results of SDS-PAGE, MALDI-TOF MS and gel filtration analysis of HML indicated that the lectin was a dimer with each subunit of 9.5 kDa. The partial amino acid sequences of HML were determined by N -terminal sequencing of peptides obtained by trypsin or Glu-C endopeptidase digest of the lectin. In the hemagglutination inhibition assay, HML did not bind to any mono- or oligo-saccharides tested. Among the glycoproteins examined, asialo-fetuin was the strongest inhibitor. [ABSTRACT FROM AUTHOR]
- Published
- 2015
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