SINGLE-STEP PURIFICATION OF IMMUNOGLOBULIN-M ON C1Q-SEPHAROSE

被引：22

作者：

NETHERY, A

RAISON, RL

EASTERBROOKSMITH, SB

机构：

[1] UNIV SYDNEY,CLIN IMMUNOL RES CTR,SYDNEY,NSW 2006,AUSTRALIA

[2] UNIV SYDNEY,DEPT BIOCHEM,SYDNEY,NSW 2006,AUSTRALIA

来源：

JOURNAL OF IMMUNOLOGICAL METHODS | 1990年 / 126卷 / 01期

关键词：

Chromatography affinity; Complement; 1; Immunoglobulin M; Purification;

D O I：

10.1016/0022-1759(90)90011-J

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

A rapid and simple affinity chromatography method for purifying IgM from myeloma serum and ascites fluid is described ***. Complement protein C1q is coupled to Sepharose with an efficiency of 35%, giving 1.7 mg of C1q bound/ml of gel. This C1q-Sepharose selectively binds IgM from crude samples at 5°C, with a capacity of 0.4 mg of IgM/ml of gel. The bound IgM may be eluted simply and isocratically by bringing the gel to room temperature for 2 h, or by washing with buffer containing 0.5 M KI. The eluted IgM is highly pure by SDS-PAGE and double immunodiffusion analysis, although IgM may be a potential contaminant. The C1q-Sepharose is stable for at least 18 months. © 1990.

引用

页码：57 / 60

页数：4

共 6 条

[1] TEMPERATURE-SENSITIVE BINDING OF SOLID-PHASE C1Q TO AGGREGATED HUMAN IMMUNOGLOBULIN-G [J].