| Literature DB >> 2013293 |
P Lepage1, F Bitsch, D Roecklin, E Keppi, J L Dimarcq, J M Reichhart, J A Hoffmann, C Roitsch, A Van Dorseelaer.
Abstract
The primary-structure comparison of natural insect defensin A from Phormia terranovae and recombinant insect defensin A from Saccharomyces cerevisiae has been accomplished using a combination of Edman degradation and liquid secondary ion mass spectrometry. The natural and recombinant proteins have the same primary structure with identical disulfide-bond designations (formula; see text) as determined from the peptides obtained after thermolysin digestion. The combined use of Edman degradation and mass spectometry allowed the disulfide-bridge structure to be determined with a total of only 40 micrograms (9.9 nmol) natural peptide. Mass spectrometry provides a rapid means of disulfide-bridge verification, requiring not more than 20 micrograms recombinant insect defensin A, which is compatible with use in batch analysis.Entities:
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Year: 1991 PMID： 2013293 DOI： 10.1111/j.1432-1033.1991.tb15872.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956