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.
|Number of pages||3|
|Journal||Biochimica et Biophysica Acta - General Subjects|
|State||Published - 12 Jun 1992|
Bibliographical noteFunding 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).
- (P. aeruginosa)
- Equilibrium dialysis
- Hydrophobic thiosaccharide