Specificity of the fucose-binding lectin of Pseudomonas aeruginosa

N. Garber, U. Guempel, N. Gilboa-Garber, R. J. Royle

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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.

Original languageEnglish
Pages (from-to)331-334
Number of pages4
JournalFEMS Microbiology Letters
Issue number3
StatePublished - 15 Dec 1987

Bibliographical note

Funding Information:
The authorsw ish to thank Mrs. Aviva Belz for skillful technicaal ssistance. This work was enabledb y a FulbrightF ellow-ship given to R.J. Doyle for work at Weizmann Institute,R ehovot,I srael and a sabbaticalle ave givent o N. Garberf romBar Ilan Universitys pent at Louisville, KY. This work was supportedin part by a grant from the Ohio Valley Chaptero f the March of Dimes.


  • Equilibrium dialysis
  • Hemagglutination
  • Lectin
  • Pseudomonas aeruginosa
  • α-L-Fucose


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