摘要
采用阳离子交换层析、RP-FPLC及RP-HPLC分离纯化技术,从细菌诱导的桔小实蝇蛹中分离鉴定出桔小实蝇抗菌肽Bactrocerin-1的同系物Bactrocerin-2。结果表明:Bactrocerin-2含有20个氨基酸残基,分子量为2 311.51 u,序列为VTKTWIKVIRGIGKSKIKWA;并且Bactrocerin-2与Bactrocerin-1的相似性极高,氨基酸同源性达到90%;该肽与鞘翅目Coleoptericin C-末端的20个氨基酸也具有较高的相似性。氨基酸组成分析结果表明,该肽是一种疏水、带正电荷的抗菌肽。该研究将有助于对昆虫天然免疫反应的认知,并为设计有效的抗菌分子奠定基础。
Bactrocerin -2 (20 -residues)was purified dorsalis Hendel by cation-exchange chromatography, Molecular mass of Baetroeerin-2 was determined from the immunized pupae of oriental fruit fly Bactrocera RP-FPLC and RP-HPLC. It was an isoform of Bactroeerin-1. as 2 311.51 u by MALDI-TOF-MS. Complete amino acid sequences was VTKTWIKVIRGIGKSKIKWA. It showed very high similarity to C-terminal sequences of Coleoptericin. The composition of amino acid residues revealed that Bactrocerin-2 was a hydrophobic, positively charged peptide.
出处
《热带作物学报》
CSCD
北大核心
2012年第3期556-561,共6页
Chinese Journal of Tropical Crops
基金
浙江省自然科学基金(No.Y3110597)
广东省自然科学基金(No.032256)