Abstract

A new mannan-binding lectin (MBL) and a previously described fucose-binding lectin (FBL) have been isolated from serum of Anguilla anguilla by affinity chromatography on A-peptone-Sepharose in combination with electroelution (MBL) or affinity chromatography using α- l-fucose-agarose (FBL). MBL has a mol. wt of approximately 246,000 and is composed of identical subunits of approximately 24,000, two of each are always covalently linked. FBL has a mol. wt of about 121,000 and consists of four subunits of 30,000, which, upon reduction are split into two identical subunits of 15,000. Upon isoelectric focusing MBL displays four bands ranging from pH 4.8 to 5.2 FBL shows 17–20 bands between pH 5.5 and 6.2. Of the inhibitors utilized, hemagglutination activity of MBL is inhibited only by mannan, whereas FBL activity is inhibited by several glycosubstances. MBL and FBL activity is constant between pH 4 and 10 and 5 and 10, respectively. Temperatures above 55°C totally destroy MBL activity whereas FBL activity remains constant up to 75°C.

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