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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1992-1-8
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pubmed:abstractText |
A synthetic antibody-binding part derived from protein A from Staphylococcus aureus was used as a fusion partner in a eukaryotic expression system employing Autographa californica nuclear polyhedrosis as a vector. This, in conjunction with an efficient signal sequence, facilitated the purification of the antibacterial peptide cecropin A from the medium of Spodoptera frugiperda cells infected with a recombinant virus. In order to increase further the concentrations of fusion protein, Trichoplusia ni larvae were used as host. Cecropin A could be obtained after cleavage of the fusion protein with CNBr. Biological activity as well as the correct structure including the C-terminal amide group was shown using electrophoresis with detection of antibacterial proteins and mass spectroscopy.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-15768483,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-16057320,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-1712729,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-2268291,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-2270488,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-2440339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-2497580,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-2692562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-2925637,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-3128324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-3149610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-3211139,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-3318666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-3507693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-3676250,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-3692175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-412251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-6579533,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-7019715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-7140755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-7341234,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1720614-85300
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
280 ( Pt 1)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
219-24
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:1720614-Amino Acid Sequence,
pubmed-meshheading:1720614-Animals,
pubmed-meshheading:1720614-Antimicrobial Cationic Peptides,
pubmed-meshheading:1720614-Baculoviridae,
pubmed-meshheading:1720614-Base Sequence,
pubmed-meshheading:1720614-Binding Sites, Antibody,
pubmed-meshheading:1720614-Blotting, Northern,
pubmed-meshheading:1720614-Cell Line,
pubmed-meshheading:1720614-Chromatography, High Pressure Liquid,
pubmed-meshheading:1720614-Genetic Vectors,
pubmed-meshheading:1720614-Hemolymph,
pubmed-meshheading:1720614-Insect Hormones,
pubmed-meshheading:1720614-Insects,
pubmed-meshheading:1720614-Mass Spectrometry,
pubmed-meshheading:1720614-Molecular Sequence Data,
pubmed-meshheading:1720614-Moths,
pubmed-meshheading:1720614-Peptide Fragments,
pubmed-meshheading:1720614-RNA,
pubmed-meshheading:1720614-Recombinant Fusion Proteins,
pubmed-meshheading:1720614-Restriction Mapping,
pubmed-meshheading:1720614-Staphylococcal Protein A,
pubmed-meshheading:1720614-Transfection
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pubmed:year |
1991
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pubmed:articleTitle |
Biologically active and amidated cecropin produced in a baculovirus expression system from a fusion construct containing the antibody-binding part of protein A.
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pubmed:affiliation |
Department of Microbiology, University of Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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