摘要
采用75%乙醇沉淀、阴离子交换色谱层析和阳离子交换色谱层析等方法,分离并纯化侧孢芽孢杆菌(Bacillus laterospours)2-Q-9菌株外泌抗菌肽BL2Q9。结果表明,BL2Q9的相对分子质量为7 800,等电点为10.2。Edman降解测序发现其N末端封闭,串联质谱测序结果表明其与细菌第Ⅳ类鞭毛合成蛋白pilQ的前体蛋白以及转录抑制子CodY蛋白的部分序列相似,但与已知抗菌肽的序列相似性较低。
Bacillus laterosporus stranin 2？Q？9 secreted a high level of antimicrobial peptides when cells were grown in liquid NB media at 28 ℃ for 24 h.Purification was carried out by protein precipitation with 75% ethanol,anion-exchange chromatography and cation-exchange chromatography sequentially.The relative molecular weight and isoletric point of antimicrobial peptide BL2Q9 were 7 800 and 10.2 respectively.The sequencing results of MS/MS showed that the antimicrobial peptide was a new antimicrobial peptide（AMP） with low amino acid sequence similarity among the known AMPs in database.
出处
《湖南农业大学学报（自然科学版）》
CAS
CSCD
北大核心
2011年第1期26-30,共5页
Journal of Hunan Agricultural University(Natural Sciences)
基金
湖南省自然科学基金项目(BK0431)
湖南省教育厅青年项目(03B012)
关键词
侧孢芽孢杆菌
外泌抗菌肽
纯化与鉴定
质谱测序
Bacillus laterosporus
antimicrobial peptide
purification and characterization
mass spectrometry/mass spectrometry
