Purification and characterization of the Dr hemagglutinins expressed by two uropathogenic Escherichia coli strains.
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Kist ML, Salit IE, Hofmann T
Purification and characterization of the Dr hemagglutinins expressed by two uropathogenic Escherichia coli strains.
Infect Immun. 1990 Mar;58(3):695-702.
- PubMed ID
- 1968432 [ View in PubMed]
- Abstract
The fibrillar Dr hemagglutinins expressed by two uropathogenic Escherichia coli isolates were mechanically sheared from whole cells and subsequently purified by using anion-exchange high-pressure liquid chromatography. The isolated hemagglutinins were proteins with apparent subunit molecular masses of 14,500 daltons by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric points of 5.4 in denaturing isoelectric focusing gels. The two proteins were serologically related to each other but distinct from P fimbriae, as assessed by bacterial agglutination and immunoblotting. The amino acid compositions of the two hemagglutinins were highly similar both to each other and to other Dr hemagglutinins. N-terminal amino acid sequencing of the major hemagglutinin subunit proteins demonstrated homology with afimbrial E. coli adhesins.