ANTIFUNGAL PROTEIN

摘要

For the first time, a small cystine rich protein (AFPl-Ca) secreted from the germinating seeds of a legume plant, chickpea (Cicer arietinum, L) with antifungal activity has been identified, purified and characterized the encoding gene cloned. The purified protein inhibited the growth of Pythium aphanidermatum mycelium at an IC50 value of 12 µg/ml. The SDS-PAGE analysis indicated the presence of disulfide bridges and a prior treatment of purified AFPl-Ca with a reducing agent, ß- mercaptoethanol, abolished the antifungal activity completely. The complete gene coding for the AFPl-Ca was isolated, DNA sequenced and the deduced amino acid sequence revealed that the gene code for (74) amino acids; (27) amino acids of signal peptide and (47) amino acids of mature protein.