为了解牛血红蛋白源抗菌肽BHP’的基本信息,试验通过软件对BHP的生物信息学进行了分析。结果表明:BHP的等电点为9.53,分子质量为3206.61u,静电荷为2;为稳定的亲水多肽,定位于细胞外;没有跨膜区和信号肽,没有糖基化位点,有5个磷酸化位点和1个泛素化位点;二级结构主要由无规则卷曲组成,存在多个酶切位点。说明牛血红蛋白源抗菌肽BHP可与细菌细胞膜作用,从而致菌体死亡。
A study was conducted to research the basic information of antimicrebial peptide BHP from bovine hemoglobin. Bioinformatics tools on line was used to analyzed according to the amino acid sequence. The results showed that the isoelectric point was 9.53, the molecular weight was 3 206.61 u, and the electrostatic charge was 2. BHP was the stable and hydrephilic peptide, which located in extracellular. BHP did not manifested transmembrane domain, signal peptide and glyeosylation site. And that manifested 5 phosphorylation sites and 1 ubiquitination site. The secondary structure of BHP was mainly composed of random coil, which manifested several restriction enzyme cutting sites. It was conclu- ded that AMP BHP of bovine hemoglobin interacted with the cell membrane, caused the death of bacteria.