Wagner R C, Kreiner P, Barrnett R J, Bitensky M W
Proc Natl Acad Sci U S A. 1972 Nov;69(11):3175-9. doi: 10.1073/pnas.69.11.3175.
Capillaries were isolated from epididymal fat, and a catecholamine-sensitive adenylate cyclase found in these capillaries was characterized. The effect of various hormones on the accumulation of adenosine 3':5'-cyclic monophosphate in capillary endothelial cells was determined and the cyclase was found to exhibit mixed alpha and beta characteristics. Cyclase was cytochemically localized in these endothelial cells with 5'-adenylyl-imidodiphosphate as a specific cyclase substrate and alloxan as a specific cyclase inhibitor. Lead imidodiphosphate was precipitated at or near the site of cyclase activity upon hydrolysis of 5'-adenylyl-imidodiphosphate by cyclase. This reaction product was observed primarily on the luminal surface of intact capillaries, in micropinocytic invaginations, in free vesicles within the cytoplasm, and in the intracellular junctions.
从附睾脂肪中分离出毛细血管，并对这些毛细血管中发现的一种对儿茶酚胺敏感的腺苷酸环化酶进行了特性鉴定。测定了各种激素对毛细血管内皮细胞中3':5'-环磷酸腺苷积累的影响，发现该环化酶具有混合的α和β特性。以5'-腺苷酰亚胺二磷酸作为特异性环化酶底物，四氧嘧啶作为特异性环化酶抑制剂，通过细胞化学方法将环化酶定位在这些内皮细胞中。当环化酶水解5'-腺苷酰亚胺二磷酸时，焦磷酸铅在环化酶活性部位或其附近沉淀。这种反应产物主要在完整毛细血管的管腔表面、微吞饮内陷、细胞质内的游离小泡以及细胞间连接处观察到。
