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Characteristics and antifungal activity of a chitin binding protein from Ginkgo biloba
Author(s) -
Huang Xu,
Xie Wei-jun,
Gong Zhen-zhen
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01834-2
Subject(s) - ginkgo biloba , edman degradation , hypha , biochemistry , cysteine , fusarium , alternaria alternata , chemistry , molecular mass , chitin , amino acid , peptide sequence , biology , microbiology and biotechnology , botany , enzyme , chitosan , gene
An antifungal peptide from leaves of Ginkgo biloba , designated GAFP, has been isolated. Its molecular mass of 4244.0 Da was determined by mass spectrometry. The complete amino acid sequence was obtained from automated Edman degradation. GAFP exhibited antifungal activity towards Pellicularia sasakii Ito, Alternaria alternata (Fries) Keissler, Fusarium graminearum Schw. and Fusarium moniliforme . Its activities differed among various fungi. GAFP could also cause increased hyphal membrane permeabilization and a rapid alkalization of the medium when applied at 100 μg/ml to Pellicularia sasakii Ito hyphae. The amino acid sequence of GAFP shows characteristics of the cysteine/glycine‐rich chitin binding domain of many chitin binding proteins. The cysteine residues are well conserved.