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Purification of the murine heat-stable antigen from erythrocytes
Y Hitsumoto1, A Nakano, H Ohnishi
1Department of Clinical Laboratory Medicine, Ehime University School of Medicine, Japan.
Biochemical and Biophysical Research Communications
|September 16, 1992
Abstract:
The rat anti-mouse erythrocyte (MRBC) monoclonal antibody (mAb), R13, has been developed. The MRBC membrane protein recognized by R13 (R13-Ag) can be purified 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.