摘要
以低渗沉淀方法制备的豚鼠血清功能纯C1及人血清为实验材料,建立C2溶血活性检测方法,经CM-SephadexC50离子交换色谱分离纯化豚鼠血清功能纯C2分子。经鉴定,所得功能纯C2具有良好活性,无C1及C3~C9活性成份,可用于体外组装经典途径C3转化酶。本工作为进一步研究经典途径C3转化酶的补体调控蛋白奠定了基础。
Haemolytic assays for the second component of complement was established by using human fresh serum and functionally pure C1 gp prepared by euglobulin precipitatoin. Functionally pure C2 without C1 and C3~C9 activity was prepared by ion exchange chromatography on CM Sephadex C50. Assembly of the classical pathway C3 convertase in vitro using functionally pure gp C1, gp C2 and EAC4 hu enable us to further investigate the function of complement regulatory proteins.
出处
《免疫学杂志》
CAS
CSCD
北大核心
1999年第1期57-60,共4页
Immunological Journal
基金
国家自然科学基金