Volume 3, Issue 3 And 4 (7-1999)                   IBJ 1999, 3(3 And 4): 89-91 | Back to browse issues page

XML Print


Abstract:  
Prostate-specific antigen (PSA) was purified to homogeneity from human seminal plasma by ion-exchange chromatography on a CM-Sephadex C-50 and by gel filtration on a Sephacryl S-200 column. A single 33-kDa protein band appeared in SDS-PAGE. High pressure liquid chromatography (HPLC) of the purified protein produced a single peak, while isoelectric focusing demonstrated the presence of five different isoforms of this protein. The immunoreactivity of the purified PSA was checked by Western blotting. This simple two-step method can be used for a large-scale preparation of the purified PSA for the clinical tests and also for further investigative studies on the biological properties of this protein.
Type of Study: Full Length/Original Article |

Rights and permissions
Creative Commons License This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.