PURIFICATION OF THE MURINE HEAT-STABLE ANTIGEN FROM ERYTHROCYTES

被引：8

作者：

HITSUMOTO, Y

NAKANO, A

OHNISHI, H

HAMADA, F

SAHEKI, S

TAKEUCHI, N

机构：

[1] OSAKA UNIV,MICROBIAL DIS RES INST,DEPT ONCOGENE RES,SUITA,OSAKA 565,JAPAN

[2] EHIME UNIV,SCH MED,DEPT ANESTHESIOL,SHIGENOBU,EHIME 79102,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 187卷 / 02期

关键词：

D O I：

10.1016/0006-291X(92)91262-O

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The rat anti-mouse erythrocyte (MRBC) monoclonal antibody (mAb), R13, has been developed. The MRBC membrane protein recognized by R13 (R13-Ag) can be pirified by loading the butanol-extracted MRBC membrane solution on a R13-conjugated Cellulofine column in the presence of 0.1% CHAPS followed by elution with 1% CHAPS. The amino acid sequence of the affinity-purified R13-Ag corresponded to that predicted from the cDNA for the murine heat-stable antigen. It was revealed that the actual heat-stable antigen was composed of 27 amino acids. © 1992.

引用

页码：773 / 777

页数：5

共 9 条

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