title: Studies on the murine Ss protein. I. Purification, molecular weight, and subunit structure.
abstract: The murine Ss protein has been isolated and purified. Using specific antisera, the radiolabeled protein has a mol wt of 120,000 in sodium dodecyl sulfate polyacrylamide gels. It is composed of two basic subunits of 23,000 and 14,000 daltons. The smaller molecular weight subunit contains a single disulfide bridge, is devoid of carbohydrate, and may represent the murine equivalent of beta2-microglobulin.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D001798:Blood Proteins / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002874:Chromosome Mapping; D004591:Electrophoresis, Polyacrylamide Gel; D006649:Histocompatibility Antigens; D005779:Immunodiffusion; D051379:Mice; D008811:Mice, Inbred DBA; D008968:Molecular Conformation; D008970:Molecular Weight
chemical_list: D000906:Antibodies; D001798:Blood Proteins; D006649:Histocompatibility Antigens