摘要
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。
One arginine esterase has been purified from Chinese Agkistrodon blomhoffii Ussurensis venom by using DEAE Sephadex A-50 ion-exchange and Sephadex G-75 gel filtration chromatography.This kind of enzyme was found to be in high homogeneity determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and matrix-assisted laser desorption/ionization,time of flight,mass spectrometry(MALDI/TOF/MS).The arginine esterase was determined to have a molecular weight of 29918.5±15 Da.All the results offered reliable information for further study on the structural and biological activities of this enzyme.
出处
《化学研究》
CAS
2000年第1期1-4,共4页
Chemical Research
基金
吉林省科委资助!项目 ( 962 90 7)
关键词
蛇毒
精氨酸酯酶
纯化
分子量测定
纯度
Agkistrodon blomhoffii Ussurensis venom
arginine esterase
purification
