On the specificity of the d-galactose-binding lectin (PA-I) of Pseudomonas aeruginosa and its strong binding to hydrophobic derivatives of d-galactose and thiogalactose

Nachman Garber; Ulrike Guempel; Aviva Belz; Nechama Gilboa-Garber; Ronald J. Doyle

doi:10.1016/0304-4165(92)90048-Y

On the specificity of the d-galactose-binding lectin (PA-I) of Pseudomonas aeruginosa and its strong binding to hydrophobic derivatives of d-galactose and thiogalactose

Nachman Garber, Ulrike Guempel, Aviva Belz, Nechama Gilboa-Garber, Ronald J. Doyle

The Mina and Everard Goodman Faculty of Life Sciences

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

66 Scopus citations

Abstract

The d-galactose-binding lectin (PA-I) from the bacterium Pseudomonas aeruginosa, isolated by affinity chromatography on Sepharose, was examined for its relative affinities for simple sugars and their derivatives using equilibrium dialysis and hemagglutination inhibition tests. The lectin, which was found to bind 0.68 mol of d-galactose per subunit of 12.8 kDa, exhibited an association constant (K_a) of 3.4·10⁴ M^-1 for d-galactose and higher affinities for hydrophobic and thio derivatives of d-galactose (with highest affinity for the hydrophobic thio derivatives). α-Methyl-galactoside was a stronger inhibitor than the β-methyl derivative and α-lactose was a weak inhibitor but the hydrophobic phenylated derivatives of the β-configuration of d-galactose were more potent inhibitors than the respective α-galactosides.

Original language	English
Pages (from-to)	331-333
Number of pages	3
Journal	Biochimica et Biophysica Acta - General Subjects
Volume	1116
Issue number	3
DOIs	https://doi.org/10.1016/0304-4165(92)90048-Y
State	Published - 12 Jun 1992

Bibliographical note

Funding Information:
This work was made possibleb y a sabbaticalle ave given to Professor N. Gather to work at Louisville UniversityK, Y, The researchw ass upportedin part by grantsf romthe March of Dimes (Ohio Valley Chapter) and the U.S.-Israel Bi-Natioual Science Foundation (BSF), JerusalemI,s rael(Grant No. 89.00454).

Keywords

(P. aeruginosa)
Equilibrium dialysis
Hemagglutination
Hydrophobic thiosaccharide
Lectin
d-Galactose

Access to Document

10.1016/0304-4165(92)90048-Y

Cite this

@article{da604d3d395f42fab7674ba772e06ff9,

title = "On the specificity of the d-galactose-binding lectin (PA-I) of Pseudomonas aeruginosa and its strong binding to hydrophobic derivatives of d-galactose and thiogalactose",

abstract = "The d-galactose-binding lectin (PA-I) from the bacterium Pseudomonas aeruginosa, isolated by affinity chromatography on Sepharose, was examined for its relative affinities for simple sugars and their derivatives using equilibrium dialysis and hemagglutination inhibition tests. The lectin, which was found to bind 0.68 mol of d-galactose per subunit of 12.8 kDa, exhibited an association constant (Ka) of 3.4·104 M-1 for d-galactose and higher affinities for hydrophobic and thio derivatives of d-galactose (with highest affinity for the hydrophobic thio derivatives). α-Methyl-galactoside was a stronger inhibitor than the β-methyl derivative and α-lactose was a weak inhibitor but the hydrophobic phenylated derivatives of the β-configuration of d-galactose were more potent inhibitors than the respective α-galactosides.",

keywords = "(P. aeruginosa), Equilibrium dialysis, Hemagglutination, Hydrophobic thiosaccharide, Lectin, d-Galactose",

author = "Nachman Garber and Ulrike Guempel and Aviva Belz and Nechama Gilboa-Garber and Doyle, {Ronald J.}",

note = "Funding Information: This work was made possibleb y a sabbaticalle ave given to Professor N. Gather to work at Louisville UniversityK, Y, The researchw ass upportedin part by grantsf romthe March of Dimes (Ohio Valley Chapter) and the U.S.-Israel Bi-Natioual Science Foundation (BSF), JerusalemI,s rael(Grant No. 89.00454).",

year = "1992",

month = jun,

day = "12",

doi = "10.1016/0304-4165(92)90048-Y",

language = "אנגלית",

volume = "1116",

pages = "331--333",

journal = "Biochimica et Biophysica Acta - General Subjects",

issn = "0006-3002",

publisher = "Elsevier",

number = "3",

}

On the specificity of the d-galactose-binding lectin (PA-I) of Pseudomonas aeruginosa and its strong binding to hydrophobic derivatives of d-galactose and thiogalactose. / Garber, Nachman; Guempel, Ulrike; Belz, Aviva et al.
In: Biochimica et Biophysica Acta - General Subjects, Vol. 1116, No. 3, 12.06.1992, p. 331-333.

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

TY - JOUR

T1 - On the specificity of the d-galactose-binding lectin (PA-I) of Pseudomonas aeruginosa and its strong binding to hydrophobic derivatives of d-galactose and thiogalactose

AU - Garber, Nachman

AU - Guempel, Ulrike

AU - Belz, Aviva

AU - Gilboa-Garber, Nechama

AU - Doyle, Ronald J.

N1 - Funding Information: This work was made possibleb y a sabbaticalle ave given to Professor N. Gather to work at Louisville UniversityK, Y, The researchw ass upportedin part by grantsf romthe March of Dimes (Ohio Valley Chapter) and the U.S.-Israel Bi-Natioual Science Foundation (BSF), JerusalemI,s rael(Grant No. 89.00454).

PY - 1992/6/12

Y1 - 1992/6/12

N2 - The d-galactose-binding lectin (PA-I) from the bacterium Pseudomonas aeruginosa, isolated by affinity chromatography on Sepharose, was examined for its relative affinities for simple sugars and their derivatives using equilibrium dialysis and hemagglutination inhibition tests. The lectin, which was found to bind 0.68 mol of d-galactose per subunit of 12.8 kDa, exhibited an association constant (Ka) of 3.4·104 M-1 for d-galactose and higher affinities for hydrophobic and thio derivatives of d-galactose (with highest affinity for the hydrophobic thio derivatives). α-Methyl-galactoside was a stronger inhibitor than the β-methyl derivative and α-lactose was a weak inhibitor but the hydrophobic phenylated derivatives of the β-configuration of d-galactose were more potent inhibitors than the respective α-galactosides.

AB - The d-galactose-binding lectin (PA-I) from the bacterium Pseudomonas aeruginosa, isolated by affinity chromatography on Sepharose, was examined for its relative affinities for simple sugars and their derivatives using equilibrium dialysis and hemagglutination inhibition tests. The lectin, which was found to bind 0.68 mol of d-galactose per subunit of 12.8 kDa, exhibited an association constant (Ka) of 3.4·104 M-1 for d-galactose and higher affinities for hydrophobic and thio derivatives of d-galactose (with highest affinity for the hydrophobic thio derivatives). α-Methyl-galactoside was a stronger inhibitor than the β-methyl derivative and α-lactose was a weak inhibitor but the hydrophobic phenylated derivatives of the β-configuration of d-galactose were more potent inhibitors than the respective α-galactosides.

KW - (P. aeruginosa)

KW - Equilibrium dialysis

KW - Hemagglutination

KW - Hydrophobic thiosaccharide

KW - Lectin

KW - d-Galactose

UR - http://www.scopus.com/inward/record.url?scp=0026718835&partnerID=8YFLogxK

U2 - 10.1016/0304-4165(92)90048-Y

DO - 10.1016/0304-4165(92)90048-Y

M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???

C2 - 1610890

AN - SCOPUS:0026718835

SN - 0006-3002

VL - 1116

SP - 331

EP - 333

JO - Biochimica et Biophysica Acta - General Subjects

JF - Biochimica et Biophysica Acta - General Subjects

IS - 3

ER -

On the specificity of the d-galactose-binding lectin (PA-I) of Pseudomonas aeruginosa and its strong binding to hydrophobic derivatives of d-galactose and thiogalactose

Abstract

Bibliographical note

Keywords

Access to Document

Other files and links

Fingerprint

Cite this