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  • Title: Characterization and partial purification of a lectin from the hemolymph of the white shrimp Litopenaeus schmitti.
    Author: Cominetti MR, Marques MR, Lorenzini DM, Löfgren SE, Daffre S, Barracco MA.
    Journal: Dev Comp Immunol; 2002 Oct; 26(8):715-21. PubMed ID: 12206835.
    Abstract:
    The agglutinating activity of the hemolymph of Litopenaeus schmitti is insensitive to calcium and specific for acetylated sugars, particularly sialic acid (Neu5Ac) and O-sialoglycoconjugates (bovine submaxillary mucin) and has varying specificity for different LPS, which may suggest a putative role in microorganism recognition. Affinity chromatography on fetuin-agarose of the agglutinin resulted in a 220 kDa band (lectin), and a 82.5 kDa band, which probably is hemocyanin. The 220 kDa protein consists of 31 and 34 kDa subunits, suggesting that this lectin is multimeric. The lectin molecular mass was estimated by gel filtration to be 153+/-10 kDa. The hemolymph of L. schmitti comprises at least another soluble lectin, with distinct chemical and carbohydrate specificity than the 220 kDa lectin.
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