Kugler P
Histochemistry. 1982;76(4):557-66. doi: 10.1007/BF00489910.
The activity of the lysosomal dipeptidyl aminopeptidase II (DAP II) was measured by quantitative histochemical methods in the S1/S2 segments of the proximal tubule using freeze dried and celloidin mounted cryostat sections (FDC sections) of rat kidney. The methodological studies show that there is a linear relationship between the amount of reaction product and reaction time for the first 5 min, as well as section thickness between 4 and 10 microns. Maximal DAP II activities were demonstrated at pH 5.5. The Km of DAP II was about 2.3 mM. In addition to the methodological studies, DAP II activity was also measured in the proximal tubule (S1/S2 segments) of experimental animals (sham-operated and castrated male and female rats). Sham-operated females showed significantly higher DAP II activities than males. DAP II activity increased significantly in castrated males so that there were no significant differences between castrated males, sham-operated and castrated females. The quantitative histochemical results are largely in agreement with biochemical data published earlier.
采用定量组织化学方法，利用大鼠肾脏的冻干火棉胶包埋冰冻切片（FDC切片），测定近端小管S1/S2段溶酶体二肽基氨基肽酶II（DAP II）的活性。方法学研究表明，在前5分钟内，反应产物量与反应时间以及4至10微米的切片厚度之间存在线性关系。DAP II在pH 5.5时表现出最大活性。DAP II的Km约为2.3 mM。除了方法学研究外，还对实验动物（假手术和去势的雄性和雌性大鼠）的近端小管（S1/S2段）进行了DAP II活性测定。假手术雌性大鼠的DAP II活性显著高于雄性。去势雄性大鼠的DAP II活性显著增加，以至于去势雄性大鼠、假手术和去势雌性大鼠之间没有显著差异。定量组织化学结果与早期发表的生化数据基本一致。
