Müntzing J, Saroff J, Sandberg A A, Murphy G P
Urology. 1978 Mar;11(3):278-82. doi: 10.1016/0090-4295(78)90136-x.
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.
对可移植的R - 3327大鼠前列腺腺癌中酸性磷酸酶、碱性磷酸酶、非特异性酯酶、β - 葡萄糖醛酸酶和氨肽酶的活性及分布进行了检测，并与大鼠四个前列腺叶中的这些酶进行了比较。R - 3327癌中高分化和低分化肿瘤细胞均具有高活性的β - 葡萄糖醛酸酶和氨肽酶。低分化细胞具有高碱性磷酸酶活性。R - 3327腺癌的酶谱与前列腺前叶和背叶的酶谱非常相似。肿瘤可能起源于这些前列腺叶中的某一个，但尚不能确定。
