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PA‐II lectin of Pseudomonas aeruginosa, purified by affinity chromatography, was examined for its relative affinity to various carbohydrates using equilibrium dialysis and hemagglutination inhibition tests. This lectin was found to exhibit a high affinity for L‐fucose and its derivatives. Among them, p‐nitrophentl‐α‐L‐fucose was the strongest inhibitor, followed by L‐fucose →L‐fucosylamine L‐galactose →D‐mannose →?→D‐fructose. The association constant (Ka) of L‐focuse for PA‐II was 1.5 × 106· M−1 and the number of the L‐fucose‐binding sites per protein subunit was approximately 1. The Ka of D‐mannose for PA‐II was 3.1 × 10−2· M−1 and a value of 0.84 was obtained as the number of its binding sites per mole protein subunit.

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