抄録
Guanine deaminase (guanase: EC 3.5.4.3.) was purified using a previously reported method. Anti-human liver guanase rabbit serum formed a single precipitin line with the partially purified enzyme. The antiserum also completely inhibited the guanase activity of the extract.
In the immunohistochemical study employing horse radish peroxidase complexes, the DAB (3.3'-diaminobenzidine tetrahydrochloride) reaction was positive at the same site where the histochemical reaction for guanase was positive; and the control reaction using the nonimmune rabit serum in place of antibody was negative. Moreover, the biochemical data indicated that the guanase activity was located in the proximal tubule. Thus, the DAB reaction appears to accurately show the location of guanase itself. This immunohistochemical procedure for guanase should become a valuable tool in clinical studies on this enzyme.
