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Isolation, Purification, and Characterization of a Lectin from Synapta sp
Abstract:
A survey was conducted on 32 species of marine invertebrates collected in three Philippine provinces; namely, Leyte, Samar, and Batangas, as source of lectin. Among the non-food invertebrates, Synapta sp., class Holothuriodea, family Synaptidae, gave the highest aggulination titer; hence, it was chosen for further purification.
Purification was done by gel chromatography using Sephadex G-200 and affinity chromatography using fetuin-agarose column. The molecular weight of gel chromatography purified lectin (GCPL) was ~51 kDa while that of the affinity chromatography purified lectin (ACPL) was ~37 kDa. SDS-PAGE, under reducing and non-reducing conditions, gave a single sharp band with a molecular weight of ~28 kDa and ~40 kDa, respectively. Both lectins were human blood type non-specific, and also agglutinated sheep, goat, and chicken erythrocytes. The glycosylated nature of both lectins was verified by periodic acid-Schiff (PAS) staining, total carbohydrate content, and gas chromatography. Addition of divalent metal cations, calcium, and magnesium increased the activity. The lectins were temperature-dependent, with optimum activity at 10-20°C and exhibited maximum stability at pH 5-10. Both lectins also possess antibacterial and larvicidal properties but had no seed germination inhibitory property. Analysis of the N-terminal amino acid sequence of the affinity chromatography purified lectin revealed distantly related homologies to several organisms.