摘要
作者用苯-琼脂糖(Phenyl-Sepharose)亲和层析等方法从猪大脑组织中分离纯化出钙调素。经鉴定,PAGE板电泳呈现一条带;产率:4.2mg/100g大脑;分子量,经SDS-PAGE测定为14.1±1.0kd(含1mmol/L CaCl_2)和164.9±1.2kd(含1mmol/L EGTA),pI=4.35;对猪脑依赖钙调素磷酸二酯酶激活6.5倍,其激活作用被三氟拉嗪抑制。
The calmodulin has purified by heating,phenyl-Sepharose affinity chromatography,DEAE-cellulose chromatography andSephadex G_(50) chromatography from theporcine brain and characterized.The resultsshowed that the purified calmodulin appearsjust one band on PAGE slab with M.W.of14.1±1.0 kd (containing 1 mmol/L CaCl_2)and 16.9±1.2 kd (containing 1 mmol/LEGTA). Electrophoresis migration wasdistinctly different between the samplecontaining CaCl_2 and the sample containingEGTA; pI=4.35; the quantity of calmodulinrequired for half maximum activation of2800 unit of PDE was 15ng. The purifiedcalmodulin increased the activity of PDEand this action was inhibited by trifluoper-azine. The yield was 4.2 mg/100g of theporcine brain.
出处
《华西医科大学学报》
CAS
CSCD
1989年第3期235-238,共4页
Journal of West China University of Medical Sciences
基金
国家自然科学基金
关键词
钙调素
磷酸二酯酶
猪脑
Calmodulin
Phosphodiesterase
Affinity chromatography
