Isolation and purification of a rat liver-specific antigen from hepatocyte membrane.
A rat liver-specific antigen (RLSA) solubilized with the nonionic detergent non-anonyl-N-methylglucamide was purified through affinity column chromatography with a monoclonal antibody and by high-performance liquid chromatography with a hydroxylapatite column. The purified RLSA showed a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and its molecular weight was determined to be 105,000 in the presence of 2-mercaptoethanol. The antigen was reactive to the Schiff reagent and contained glucosamine, but not galactosamine, indicating that the RLSA is a glycoprotein containing an asparagine-binding type of sugar chain.
Sato
K
K
Research Institute, Daiichi Seiyaku Co., Ltd., Tokyo.
Ikeda
T
T
Kawai
F
F
Osada
Y
Y
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000954:Antigens, Surface / Q000302:isolation & purification*; D002462:Cell Membrane / Q000276:immunology; D008099:Liver / Q000276:immunology*; D008970:Molecular Weight; D010503:Periodic Acid-Schiff Reaction; D051381:Rats; D013056:Spectrophotometry, Ultraviolet
D000596:Amino Acids; D000954:Antigens, Surface