Specificity of the fucose-binding lectin of Pseudomonas aeruginosa

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

doi:10.1111/j.1574-6968.1987.tb02619.x

Specificity of the fucose-binding lectin of Pseudomonas aeruginosa

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

The Mina and Everard Goodman Faculty of Life Sciences - at Bar-Ilan University

University of Louisville

Research output: Contribution to journal › Article › peer-review

57 Scopus citations

Abstract

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 × 10⁶ · 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.

Original language	English
Pages (from-to)	331-334
Number of pages	4
Journal	FEMS Microbiology Letters
Volume	48
Issue number	3
DOIs	https://doi.org/10.1111/j.1574-6968.1987.tb02619.x
State	Published - 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.

Funding

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.

Funders
March of Dimes Foundation

Keywords

Equilibrium dialysis
Hemagglutination
Lectin
Pseudomonas aeruginosa
α-L-Fucose

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10.1111/j.1574-6968.1987.tb02619.x

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title = "Specificity of the fucose-binding lectin of Pseudomonas aeruginosa",

abstract = "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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N1 - 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.

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N2 - 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.

AB - 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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Specificity of the fucose-binding lectin of Pseudomonas aeruginosa

Abstract

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Keywords

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