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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1998-10-6
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pubmed:abstractText |
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, A.; Bennich, H. Eur. J. Biochem. 247:614-619; 1997]. At the N-terminus P2 had approximately 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, Candida albicans, a bovine turbinate cell line, and pestivirus.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0145-305X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
387-99
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9699484-Amino Acid Sequence,
pubmed-meshheading:9699484-Animals,
pubmed-meshheading:9699484-Anti-Bacterial Agents,
pubmed-meshheading:9699484-Anti-Infective Agents,
pubmed-meshheading:9699484-Candida albicans,
pubmed-meshheading:9699484-Cell Line,
pubmed-meshheading:9699484-Chromatography, High Pressure Liquid,
pubmed-meshheading:9699484-Escherichia coli,
pubmed-meshheading:9699484-Gram-Negative Bacteria,
pubmed-meshheading:9699484-Gram-Positive Bacteria,
pubmed-meshheading:9699484-Hemolymph,
pubmed-meshheading:9699484-Lepidoptera,
pubmed-meshheading:9699484-Molecular Sequence Data,
pubmed-meshheading:9699484-Molecular Weight,
pubmed-meshheading:9699484-Pestivirus,
pubmed-meshheading:9699484-Protein Biosynthesis,
pubmed-meshheading:9699484-Proteins,
pubmed-meshheading:9699484-Sequence Homology, Amino Acid
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pubmed:articleTitle |
A gloverin-like antibacterial protein is synthesized in Helicoverpa armigera following bacterial challenge.
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pubmed:affiliation |
School of Biological Sciences, Macquarie University, Sydney, New South Wales, Australia. jmackint@rna.bio.mq.edu.au
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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