摘要
应用液-液双水相提取、DEAE-纤维素层析及SIPI-I红色染料配基层析等方法提纯兔肌匀浆粗提取液中的α-磷酸甘油脱氢酶,其比活15u/mg蛋白,为原酶的50倍,总收率约50％。并对其分子量、米氏常数、酶作用的最适pH、最适温度,对pH和热的稳定性等性质作了测定。
α-Glycerophosphate dehydrogenase from rabbit muscle crude extract
was purified in sequence by means of liquid-liquid two-phase extraction, DEAE-
cellulose column chromatography and SIPI-I red dye-ligand chromatography. The
purity of enzyme was increased 50-fold with total activity recovery of 50% and
specific activity of 15u/mg protein. Its molecular weight, Km, optimum pH and
temperature and others were determined.
出处
《中国医药工业杂志》
CAS
CSCD
北大核心
1990年第6期241-244,共4页
Chinese Journal of Pharmaceuticals
关键词
磷酸甘油
脱氢酶
兔肌
提纯
rabbit muscle
α-glycerophosphate dehydrogenase
liquid-liquid two-phase extraction
red dye-ligand chromatography
