Open AccessSpecificity of the fucose‐binding lectin of Pseudomonas aeruginosa
Author(s) -
Garber N.,
Guempel U.,
GilboaGarber N.,
Royle R.J.
Publication year - 1987
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1987.tb02619.x
Subject(s) - fucose , lectin , pseudomonas aeruginosa , mannose , biochemistry , protein subunit , chemistry , ficolin , galactose , affinity chromatography , fructose , biology , microbiology and biotechnology , mannan binding lectin , bacteria , enzyme , genetics , gene
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 ( K a ) of L ‐focuse for PA‐II was 1.5 × 10 6 · M −1 and the number of the L ‐fucose‐binding sites per protein subunit was approximately 1. The K a 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.