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Publication : Purification of the murine heat-stable antigen from erythrocytes.

First Author  Hitsumoto Y Year  1992
Journal  Biochem Biophys Res Commun Volume  187
Issue  2 Pages  773-7
PubMed ID  1530634 Mgi Jnum  J:125146
Mgi Id  MGI:3757625 Doi  10.1016/0006-291x(92)91262-o
Citation  Hitsumoto Y, et al. (1992) Purification of the murine heat-stable antigen from erythrocytes. Biochem Biophys Res Commun 187(2):773-7
abstractText  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.
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