| Literature DB >> 8246255 |
Y Sakurai1, H Suzuki, E Terada.
Abstract
A surface protein of Bordetella bronchiseptica was purified in one step by affinity chromatography with bovine submaxillary mucin coupled to agarose. The purified protein, with a mol. wt of 200 kDa and an iso-electric point of pI 6.5, showed haemagglutinating activity for bovine erythrocytes. This haemagglutinin (HA) inhibited the adherence of B. bronchiseptica to a rat lung cell line (L2) and was able to bind to N-acetylneuraminic acid. These findings suggest that the HA of B. bronchiseptica is an adhesin.Entities:
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Year: 1993 PMID： 8246255 DOI： 10.1099/00222615-39-5-388
Source DB: PubMed Journal: J Med Microbiol ISSN： 0022-2615 Impact factor: 2.472