Characteristics and antifungal activity of a chitin binding protein from Ginkgo biloba

FEBS Letters

Huang, Xu¹  Gong, Zhen-zhen¹  Xie, Wei-jun¹ 

[1] Shanghai Institute of Biochemistry, Chinese Academy of Sciences, 320 Yue-yang Road, Shanghai 200031, PR China

关键词: Antifungal peptide;    Chitin;    Membrane permeabilization;    Chitinase;    Ginkgo biloba;   

DOI  :  10.1016/S0014-5793(00)01834-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown