Purification of the murine heat-stable antigen from erythrocytes.
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.
Hitsumoto
Y
Y
Department of Clinical Laboratory Medicine, Ehime University School of Medicine, Japan.
Nakano
A
A
Ohnishi
H
H
Hamada
F
F
Saheki
S
S
Takeuchi
N
N
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D015703:Antigens, CD; D000943:Antigens, Differentiation / Q000097:blood* / Q000737:chemistry / Q000276:immunology; D051927:CD24 Antigen; D002793:Cholic Acids; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000276:immunology*; D006031:Glycosylation; D008562:Membrane Glycoproteins; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D051381:Rats; D011919:Rats, Inbred Strains
D000911:Antibodies, Monoclonal; D015703:Antigens, CD; D000943:Antigens, Differentiation; D051927:CD24 Antigen; C497890:Cd24a protein, mouse; D002793:Cholic Acids; D008562:Membrane Glycoproteins; C028213:3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate