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Sephadex G-50、DEAE-Sephadex A50、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8.711KD,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。
Abstract:
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 molecular weight was determined to be 8.711KD by HPLC. Its PI was estimated to be 1.79 by IEF-HPCE. Amino acid analysis showed that it consists of 87 amino acids and it was rich in Gly、Asp、Pro、Glu. CONCLUSION NV-Pp-4 was a new protein purified from the water extract of Nidus Vespae.
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