Abstract
Lectin (PYL) of molecular mass 17,154.5 Da that exhibited Gal/GalNAc-specificity was isolated from the scallop Patinopecten yessoensis. The lectin was completely inactivated by heating to 60°C for 30 min, exhibited the greatest activity at pH 5–9, and was metal-independent. It was shown that the lectin was involved in the mollusk protective mechanism by agglutinating the Gram-negative bacterium Vibrio proteolyticus.
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