摘要
作者从人脑组织先分离出髓鞘,再经热有机溶剂除脂、三乙醇胺硷性液洗涤和稀酸液抽提、最后用Sephadex G-150柱层析纯化制备出人脑髓鞘硷性蛋白。经三种不同类型的聚丙烯酰胺凝胶电泳及免疫电泳证明,该产品为单一组分,并测得其分子量为18.5kd,等电点为10.6,与文献报道相符。本法具有简便快速、产量和纯度均高等优点,为人脑髓鞘硷性蛋白研究提供了可靠的手段。
A simplified procedure for isolationand purification of myelin basic protein(MBP) from human brain is described.Purified myelin from white matter wasisolated at first, then delipidated withheated organic solvents.The pellet waswashed with triethanolamine buffer andextracted with 0.01 mol/L HCl. Finallythe protein in the acidic supernatant waspurified with Sephadex G-150 column. Byusing three different PAGE and immuno-electrophoresis, the purified MBP wasidentified as a homogeneous componentwith an apparent molecular weight of18.5 kd and pI 10.6. This procedure hasthe advantage of simplicity, rapidity,high yield and purity.
出处
《华西医科大学学报》
CAS
CSCD
1990年第4期354-356,共3页
Journal of West China University of Medical Sciences
基金
四川省科委资助课题
纽约中华医学基金~~
关键词
人脑
髓鞘硷性蛋白
纯化
Human brain
Myelin basic Protein
Purification
