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- W2078477073 abstract "A bacteria inducible antibacterial protein, P2, was isolated from the old world bollworm Helicoverpa armigera. Fifth-instar larvae were injected with live Escherichia coli NCTC 8196. P2 was isolated by HPLC using reversed-phase and size-exclusion columns. In addition, P2 was isolated by an alternative method of sequential cation-exchange and reversed-phase HPLC. The structure of P2 was determined by N-terminal Edman degradation and mass spectrometry. P2 had similar mass (14.1 kDa) structure and activity to gloverin, an inducible glycine-rich antibacterial protein isolated from Hyalophora gloveri [Axén, A.; Carlsson, A.; Engström, Å.; Bennich, H. Eur. J. Biochem. 247:614-619; 1997]. At the N-terminus P2 had ∼60% identity with gloverin. P2 is basic, heat stable, and displayed rapid antibacterial action. P2 was active against the Gram-negative bacteria tested and was inactive against the Gram-positive bacteria, Candidaalbicans, a bovine turbinate cell line, and pestivirus." @default.
- W2078477073 created "2016-06-24" @default.
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- W2078477073 date "1998-07-01" @default.
- W2078477073 modified "2023-10-03" @default.
- W2078477073 title "A gloverin-like antibacterial protein is synthesized in helicoverpa armigera following bacterial challenge" @default.
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- W2078477073 doi "https://doi.org/10.1016/s0145-305x(98)00025-1" @default.
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