title: Purification of S-100a0 protein from rat kidney.
abstract: In order to corroborate our previous finding that kidney may contain a considerable amount of S-100-like antigen, concentrations of S-100a0, S-100a and S-100b antigens in rat kidney were determined by an enzyme immunoassay system, which can quantify these 3 forms of S-100 protein separately. It was revealed that rat kidney was rich in S-100a0 antigen, while it was the least occurring form in brain. To confirm the above results, S-100-like antigen in rat kidney was purified, and its physicochemical properties were compared with those of S-100 proteins of bovine brain. Electrophoretic mobility, calcium binding ability, apparent molecular weight, amino acid composition as well as elution profiles from butyl-Sepharose and anion exchange columns were similar to those of S-100a0 protein of bovine brain. These results indicate that S-100a0 protein is not a protein unique to brain, as had long been believed.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D001923:Brain Chemistry; D002118:Calcium / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D007124:Immunoenzyme Techniques; D007668:Kidney / Q000032:analysis*; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000302:isolation & purification; D011506:Proteins / Q000302:isolation & purification*; D051381:Rats; D009418:S100 Proteins / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D009419:Nerve Tissue Proteins; D011506:Proteins; D009418:S100 Proteins; D002118:Calcium