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- W4231526608 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." @default.
- W4231526608 created "2022-05-12" @default.
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- W4231526608 date "1991-03-15" @default.
- W4231526608 modified "2023-09-26" @default.
- W4231526608 title "The 20 kDa C-terminally truncated form of pertussis toxin subunit S1 secreted from Bacillus subtilis" @default.
- W4231526608 doi "https://doi.org/10.1016/0378-1097(91)90538-l" @default.
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