一种与核黄素合酶α亚基具有结构相似性的板蓝根多肽的分离纯化与表征
Isolation and characterization of peptide structural similarity with riboflavin synthase subunit alpha from radix isatidis

利用离子交换色谱SP-5PW和疏水色谱POROS HP2从板蓝根鲜根水相抽提物中分离纯化多肽组分，并对其进行生化表征. 获得一种达到电泳纯的多肽RIP2，其相对分子质量约为6.87ku，等电点约为7.73，N端氨基酸序列依次为QIGEFATAPF. 经数据库搜索比对，发现该多肽与核黄素合酶α亚基具有一定的同源性. 细胞毒性实验表明该多肽具有一定抗病毒作用.
Peptide was isolated from water extract of radix isatidis by using strong cation exchange chromatography column (SP-5PW) and hydrophobic interaction chromatography (POROS HP2)，their biochemical characters were investigated，subsequently. The peptide，which purified by using the method above，was identified to be homogeneous by Tricine-SDS-PAGE. Its relative molecular weight was estimated to be approximate 6.87ku. Its pI was estimated to be 7.73 by isoelectric focusing electrophoresis. Its N-terminal sequence was determined as QIGEFATAPF. The search in NCBI database returns that the peptide showed structural homologous with subunit alpha of riboflavin synthase. Cytotoxicity experiment demonstrated the peptide has some antiviral effect