摘要
从白鲢（Hypophthalmichthys molitrix）骨骼肌中分离纯化到一种丝氨酸蛋白酶抑制剂，该抑制剂的分子晕大约50kD，用PAGE-明胶电泳证明，该抑制剂对胰蛋白酶具有抑制作用；当温度超过60℃时，抑制剂的活性下降70％左右，但在pH3～11的范围内均有活性。用MTT法分析白鲢骨骼肌丝氨酸蛋白酶抑制剂对急性T细胞白血病细胞Jarkat、人骨髓瘤细胞Sp20和人骨瘤细胞MG63生长的影响，结果发现该抑制剂对以上3种肿瘤细胞的增殖都有抑制作用，而且抑制作用呈剂量依赖性。本研究旨为进一步研究白鲢骨骼肌丝氨酸蛋白酶抑制剂的纯化及其抗肿瘤作用提供科学依据。
A serine proteinase inhibitor was purified from silver carp （HyDophthalrnichthys molitrix） skeletal muscle by chromatographies on DEAE-Sephacel, SP-Sepharose, Blue-Sepharose and Con A-Sepharose. The purified inhibitor is a monomeric protein with the molecular mass of 50 kD as estimated by SDSPAGE. Gelatin reverse zymography showed it had inhibitory activity on trypsin. The thermal stability of the inhibitor sharply decreased at temperatures over 60℃, but showed a wide range of pH stability （pH 3- 11）. The antiproliferative effect of the purified serine proteinase inhibitor was determined by MTT on Sp20 ceils, Jarkat calls and MG63 cells. It showed the inhibition on the proliferation of the three cells in a dose-dependent manner.
出处
《中国水产科学》
CAS
CSCD
北大核心
2006年第2期316-321,共6页
Journal of Fishery Sciences of China
基金
国家自然科学基金资助项目(30371122)
关键词
丝氨酸蛋白酶抑制剂
白鲢
纯化
serine proteinase inhibitor
silver carp
purification
