摘要
目的 :从中药露蜂房抗炎活性有效部分纯化得到一酸性蛋白NV PP 4 ,并鉴定了其部分理化性质。方法 :用SephadexG 50、DEAE SephadexA50、羟基磷灰石等柱层析及HPLC等方法纯化 ,并以HPLC、毛细管等电聚焦电泳 ,氨基酸自动分析等手段 ,鉴定其理化性质。结果 :NV PP 4经不同的HPLC柱和不同的流动相匀表明为一对称单一峰、毛细管等电聚焦电泳呈单一染色带。亲水型分子排阻HPLC测定其分子量为 8 71 1KD ,毛细管等电聚焦电泳测定其等电点为 1 79,氨基酸分析表明NV PP 4含有 87个氨基酸残基 ,其中Gly、Asp、Pro、Glu等含量较多。结论 :NV PP 4是从中药露蜂房中首次分离得到的酸性蛋白质成分。
OBJECTIVE:To isolate and purify a new protein, nominated as NV PP 4 from the anti inflammatory of Nidus Vespae and study its characteristics.METHODS:It was purified by Sephadex G 50 chromatography, followed by DEAE Sephadex A50 anion exchange chromatography,hydroxyapatite column chromatography and high performance liquid chromatography,then it was characterized by HPLC,HPCE,amino acid analysis.RESULTS:HPLC and IEF HPCE showed that it was homogenous both in molecular weight and electric charge,its mole...
出处
《药学实践杂志》
CAS
2000年第5期284-285,共2页
Journal of Pharmaceutical Practice
关键词
露蜂房
酸性蛋白质
分离纯化
nisus vespae
protein
purification
characteristics
