Specific binding of lactoferrin to Aeromonas hydrophila |
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Authors: | A.R. Kishore J. Erdei S.S. Naidu E. Falsen A. Forsgren A.S. Naidu |
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Affiliation: | Molecular Biology Unit, National Public Health Institute, Helsinki, Finland. |
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Abstract: | The subunit S1 of pertussis toxin (PT) was purified as the recombinant product BacS1 from the culture supernatant of a Bacillus subtilis strain containing a secretion vector with a DNA fragment coding for the mature subunit S1 inserted downstream of the signal sequence of the alpha-amylase gene. The method of purification was successive ion exchange and adsorption chromatography. BacS1 occurred in two forms (28 and 20 kDa) of which the truncated 20-kDa peptide was the main one in the supernatant. The truncated BacS1 was purified and shown to have the same NH2-terminus as the full-size (28 kDa) BacS1. It was also enzymatically active indicating correct conformation. The truncated BacS1 was also shown to elicit neutralizing and protective antibodies when injected into mice or rabbits. |
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Keywords: | Pelobacter acidigallici Anaerobic bacterium Iron sulfide Surface Attachment |
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