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利用离子交换 (DEAESephadexA - 50 )和凝胶过滤层析 (SephadexG - 75)技术首次从长白山白眉蝮蛇蛇毒 (AgkistrodonblomhoffiiUssurensis)中纯化得到了一种精氨酸酯酶纯品。经SDS -聚丙烯酰胺凝胶电泳(SDS -PAGE)以及基质辅助激光解吸电离飞行时间质谱 (MALDI/TOF/MS)鉴定为单一纯蛋白 ,分子量为2 991 8.5± 1 5Da ,为进一步研究其结构与功能提供了可靠的依据。
A novel arginine esterase was purified from Agkistrodon bomhoffii Ussurensis for the first time using ion exchange (DEAE Sephadex A - 50) and gel filtration chromatography (Sephadex G - 75). It was identified as a single pure protein by SDS-PAGE and MALDI-TOF / MS, with a molecular weight of 2 991 8.5 ± 1 5 Da. To further investigate its structure And provide a reliable basis for the function.