Cutler L S, Christian C P
J Histochem Cytochem. 1980 Jan;28(1):62-5. doi: 10.1177/28.1.6153196.
This study examined 1) the effect of lead and fixation on adenylate cyclase activity, 2) the effect of lead on App(NH)p, and 3) the specificity of App(NH)p as a substrate for adenylate cyclase under the conditions of the cytochemical assay. The results indicated that: 1) fixation that provides adequate structural preservation inhibits enzyme activity to varying degrees depending on the tissue, fixative, length and temperature of fixation; 2) millimolar concentrations of lead do not negatively affect the adenylate cyclase activity of several different tissues (especially if 10 mM NaF is present); 3) lead does not cause the nonenzymatic hydrolysis of App(NH)p; 4) the App(NH)p obtained from the supplier is contaminated and should be purified before use, since lead can interact with the contaminants and this may be a source of error in the assay; and 5) adenylate cyclase appears to be the major enzyme that cleaves App(NH)p under cytochemical conditions.
1）铅和固定对腺苷酸环化酶活性的影响；2）铅对氨苯蝶啶（App(NH)p）的影响；3）在细胞化学检测条件下，氨苯蝶啶作为腺苷酸环化酶底物的特异性。结果表明：1）能提供充分结构保存的固定会根据组织、固定剂、固定时间和温度不同程度地抑制酶活性；2）毫摩尔浓度的铅不会对几种不同组织的腺苷酸环化酶活性产生负面影响（尤其是存在10 mM氟化钠时）；3）铅不会导致氨苯蝶啶的非酶促水解；4）从供应商处获得的氨苯蝶啶被污染，使用前应进行纯化，因为铅可与污染物相互作用，这可能是检测中的误差来源；5）在细胞化学条件下，腺苷酸环化酶似乎是裂解氨苯蝶啶的主要酶。
