Proteins of human urine. III. Identification and two-dimensional electrophoretic map positions of some major urinary proteins

We mapped the proteins of human urine by high-resolution two-dimensional electrophoresis, utilizing the ISO-DAL T system. Wide-range pH gradients and narrow-range acid gradients were both used in the first-dimension separa-tions. The patterns revealed proteins ranging in relative molecular mass from 10000 to 90000. Proteins identified in the map included transferrin, albumin, hemopexin, Ct2-HS glycoprotein, 0'1-antitrypsin, Gc globl!lin, Ct1-acid glycoprotein, Zn Ct2-glycoprotein, retinol binding protein,,82-microglobulin, the immunoglobulin light chains, and MAUP (most acid urinary protein). The use and utility of internal-charge and molecular-mass standards are de-scribed. We used electrophoretic transfer of proteins to nitrocellulose sheets and subsequent detection by im-munological methods to identify some proteins. Additional Keyphrases: ISO-OALT system. multiple myeloma. identification by transfer to nitrocellulose sheet, followed b