蒜氨酸酶与凝集素的分离纯化及质谱鉴定分析

摘要

In this study,alliinase and lectin were extracted and purified from garlic and their mass spectrometry identification was also investigated.Garlic alliinase and lectin was isolated by Sepharose Fast Flow ion exchange chromatography,and the target proteins were identified by SDS-PAGE and MALDI-TOF/MS.The results indicated that the purity of alliinase and lectin reached 90％ and 95％ respectively and was qualified for electrophoresis analysis by DEAE-Sepharose Fast Flow column purification using Tris-HC1 (50 mmol/L,pH7.2) as an extract.The results of mass spectrometry showed that the target substances were alliinase and lectin with molecular weight of 54.147 ku and 12.152 ku respectively.%对大蒜中的蒜氨酸酶和凝集素分离纯化并进行质谱分析.首次采用DEAE-Sepharose Fast Flow阴离子交换层析法对大蒜中蒜氨酸酶和凝集素进行了分离纯化,并采用SDS-PAGE电泳、MALDI-TOF/MS质谱法对目标蛋白进行了鉴定.结果表明:以Tris-HC1作为浸提液,经DEAE-Sepharose Fast Flow柱纯化的蒜氨酸酶和凝集素可达到电泳纯,质谱结果表明,所分离目标物质为蒜氨酸酶和大蒜凝集素,其分子质量分别为54.147 ku和12.152 ku.