Purification and Characterization of a Novel Rhamnose/Fucose-Specific Lectin from the Hemolymph of Oak Tasar (Antheraea proylei J.) Silkworm.

CONCLUSION: A novel rhamnose/fucose-specific lectin was purified to electrophoretic homogeneity from hemolymph of oak tasar (Antheraea proylei J.) silkworm. The lectin was found to be a monomeric protein with a native molecular weight of 39.5 kDa. Its activity was found to be independent of metal ion, optimum at pH 7-7.5 and characterized by thermal stability with t1/2 of 60°C. Analysis with tandem mass spectrometry coupled with Mascot sequence matching software confirmed the purified lectin to be a protein not characterized earlier.
PMID: 31994999 [PubMed - as supplied by publisher]

Source: Protein and Peptide Letters - January 28, 2020 Category: Biochemistry Authors: Devi HK, Devi SK, Rully H, Singh SJ, Singh WS, Thongam H, Singh LR Tags: Protein Pept Lett Source Type: research