蕲蛇毒中抑制ACE活性组分的分离纯化与表征

Purification and characterization of an angiotensin converting enzyme inhibitor from agkistrodon acutus

蕲蛇粗毒流经强阴离子交换色谱POROS 2 0HQ柱 ,经毛细管电泳仪检测 ,5个蛋白峰具有ACE抑制活性 ,对最强的活性峰进行PAGE切割电泳的分离 ,得到 3条带 ,经检测只有第三条带 (AI - 3)具有ACE抑制活性 .该组分的分子量为 2 0 2 0 0 (非还原 ) ,加DTT处理后 ,分子量为 2 590 0 .其IC50 为 0 .10mmol/L .

Protein components of Agkistrodon actutus venom in Fujian were isolated by ion-exchange chromatography on the perfusion chromatographic matrix(POROS 20 HQ), and then purified by PAGE. A main component (AI-3) of the ACE inhibitory activity detected by Capillary Zone Electrophoresis (CZE) method, which was proved to be more precise and quantitative than before, was determined to be homogeneous and its molecular weight was estimated to be 20?200 under nonreduced conditions and 25?900 under reduced conditions, both by SDS-PAGE. Its IC 50 was 2.07 mg/mL (0.10 mmol/L).