Enzyme activity and distribution in rat prostatic adenocarcinoma.
The activity and distribution of acid phosphatase, alkaline phosphatase, nonspecific esterases, beta-glucuronidase, and aminopeptidase were examined in the transplantable R-3327 rat prostatic adenocarcinoma and compared with those in the four prostatic lobes of the rat. Both the well and poorly differentiated tumor cells in R-3327 carcinoma were characterized by high activities of beta-glucuronidase and aminopeptidase. The poorly differentiated cells had a high alkaline phosphatase activity. The enzymatic profile of the R-3327 adenocarcinoma closely resembled that of the anterior and dorsal prostate. The origin of the tumor in one of these prostatic lobes is probable, but not certain.
D000230:Adenocarcinoma / Q000201:enzymology* / Q000473:pathology; D000626:Aminopeptidases / Q000378:metabolism; D000818:Animals; D005260:Female; D005966:Glucuronidase / Q000378:metabolism; D006867:Hydrolases / Q000378:metabolism*; D008297:Male; D009368:Neoplasm Transplantation; D011471:Prostatic Neoplasms / Q000201:enzymology* / Q000473:pathology; D051381:Rats
D006867:Hydrolases; D005966:Glucuronidase; D000626:Aminopeptidases