PURIFICATION AND CHARACTERIZATION OF PROSTATE-SPECIFIC ANTIGEN FROM HUMAN URINE

Prostate specific antigen (uPSA) was purified to homogeneity from huma n urine using SuperQ-Toyopearl, Sulfate-Cellulofine, Phenyl-Toyopearl, CM-Sepharose, anti-urokinase IgG Sepharose and Sephadex G-100. The pu rified uPSA gave a major band at 32.9 kDa on SDS-PAGE under the reduce d condition. However, it shows multiple bands on native PAGE. Substrat e specificity of purified uPSA is identical with that of PSA from huma n seminal plasma and uPSA shows the kallikrein and chymotrypsin-like a ctivities. On the analysis of N-terminal amino acid, two amino acid re sidues at N-terminal position of uPSA were detected and other amino ac id sequence of uPSA was identical with that of sPSA. In addition, we i solated the multiple components of uPSA using anion-exchange chromatog raphy. They were almost the same in amino acid composition and N-termi nal amino acid sequences and showed differences in lectin-blotting pat tern. (C) 1997 Elsevier Science B.V.