摘要
为研究牛源抗菌肽乳铁素的生物学功能,通过网络在线软件和工具分析了牛源抗菌肽乳铁素的生物信息学相关特性.结果表明:牛源抗菌肽乳铁素为不稳定的、带正电荷的亲水性蛋白多肽,没有跨膜区和信号肽,也没有糖基化位点和磷酸化位点,二级结构主要由α-螺旋和无规则卷曲构成,呈环形结构,定位于细胞外,可与19个蛋白分子发生相互作用.这为深入理解牛源抗菌肽乳铁素的生物学功能奠定了基础.
To research the biological function of antimicrobial peptide lactoferrcin of bovine,tools and softs on line were utilized to analyze some informatics feature of lactoferrcin of bovine.The results showed that,lactoferrcin of bovine is non-stable,positively charged,hydrophilic protein peptide,and have no transmembrane area,no signal peptide,no glycosylation sites and no phosphorylation sites.Bovine lactoferrcin mainly consists of alpha helix and random curl,and are presented as a circular structure.Lactoferrcin of bovine are located at extracellular.Lactoferrcin of bovine can interact with 19 protein molecules.This lay the foundation for an in-depth understanding of the biological functions of antimicrobial peptide lactoferrin of bovine.
作者
杭柏林
张炜
李杰
徐彦召
张慧辉
胡建和
HANG Bolin;ZHANG Wei;LI Jie;XU Yanzhao;ZHANG Huihui;HU Jianhe(College of Animal Science and Veterinary Medicine,Henan Institute of Science and Technology,Xinxiang 453003,China;Xinxiang Agriculture and Animal Husbandry Bureau,Xinxiang 453003,China)
出处
《河南科技学院学报（自然科学版）》
2018年第4期40-44,49,共6页
Journal of Henan Institute of Science and Technology(Natural Science Edition)
基金
河南省自然科学基金项目(182300410031)
河南省高校科技创新团队支持计划(15IRTSTHN)
河南科技学院高层次人才启动项目(2014020)
关键词
抗菌肽
牛
乳铁素
生物信息学
antimicrobial peptide
bovine
lactoferrcin
bioinformatics
