Abstract:
:An antifungal peptide with a molecular mass of 9412 and an N-terminal sequence exhibiting notable homology to those of lipid transfer proteins was isolated from seeds of the vegetable Brassica campestris. The purification protocol entailed ion exchange chromatography on Q-Sepharose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography by fast protein liquid chromatography (FPLC) on Mono S, and gel filtration by FPLC on a Superdex peptide column. The antifungal peptide was adsorbed on Affi-gel blue gel and Mono S. It inhibited mycelial growth in Fusarium oxysporum and Mycosphaerella arachidicola with an IC(50) value of 8.3 microM and 4.5 microM, respectively. It exhibited dose-dependent binding to lyso-alpha-lauroyl phosphatidylcholine. The present findings constitute the first report on a non-specific lipid transfer protein from the seeds of a Brassica species.
journal_name
Peptidesjournal_title
Peptidesauthors
Lin P,Xia L,Ng TBdoi
10.1016/j.peptides.2007.06.028subject
Has Abstractpub_date
2007-08-01 00:00:00pages
1514-9issue
8eissn
0196-9781issn
1873-5169pii
S0196-9781(07)00221-5journal_volume
28pub_type
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