鸡抗菌肽NK-lysin的生物信息学分析
发布时间：2018-08-17 11:56
【摘要】：为了解鸡内源性抗菌肽NK-lysin的基本信息,试验选择鸡NK-lysin的氨基酸序列通过软件对NK-lysin的生物信息学进行了分析。结果表明:NK-lysin的等电点为5.87,分子质量为15 231.3 u,为稳定蛋白和亲水蛋白,定位于细胞质内,有1个跨膜区和1个信号肽,没有糖基化位点,但有2个磷酸化位点,二级结构由α螺旋、延伸链、β折叠和无规则卷曲组成,存在多个抗原表位。说明鸡抗菌肽NK-lysin可作用于细胞膜或某些生物分子,使菌体死亡。
[Abstract]:In order to understand the basic information of chicken endogenous antimicrobial peptide (NK-lysin), the amino acid sequence of chicken NK-lysin was selected to analyze the bioinformatics of NK-lysin by software. The results showed that the isoelectric point and molecular weight of 1: NK-lysin were 5.87 and 15 231.3 u. they were stable proteins and hydrophilic proteins, located in the cytoplasm, with a transmembrane region and a signal peptide, no glycosylation sites, but two phosphorylation sites. The secondary structure consists of 伪 helix, extension chain, 尾 -fold and irregular crimp, and there are many antigenic epitopes. The results showed that chicken antimicrobial peptide NK-lysin could act on the cell membrane or some biomolecules and kill the bacteria.
【作者单位】： 河南科技学院动物科技学院;河南省新乡市畜产品质量监测检验中心;
【分类号】：S852.4
本文编号：2187554
[Abstract]:In order to understand the basic information of chicken endogenous antimicrobial peptide (NK-lysin), the amino acid sequence of chicken NK-lysin was selected to analyze the bioinformatics of NK-lysin by software. The results showed that the isoelectric point and molecular weight of 1: NK-lysin were 5.87 and 15 231.3 u. they were stable proteins and hydrophilic proteins, located in the cytoplasm, with a transmembrane region and a signal peptide, no glycosylation sites, but two phosphorylation sites. The secondary structure consists of 伪 helix, extension chain, 尾 -fold and irregular crimp, and there are many antigenic epitopes. The results showed that chicken antimicrobial peptide NK-lysin could act on the cell membrane or some biomolecules and kill the bacteria.
【作者单位】： 河南科技学院动物科技学院;河南省新乡市畜产品质量监测检验中心;
【分类号】：S852.4
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