Title: Purification and characterization of the Dr hemagglutinins expressed by two uropathogenic Escherichia coli strains. |
Journal: Infection and immunity. 1990 Mar;58(3):695-702 |
Authors: Kist ML, Salit IE, Hofmann T. |
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. |
See full PubMed entry: http://www.ncbi.nlm.nih.gov/pubmed/1968432 |