【摘要】 应用电镜酶细胞化学方法对12例胃癌细胞三磷酸腺苷酶(Mg²⁺—ATPase,Ca²⁺—ATPase),5¹—核苷酸酶（5NPase）及胞嘧啶单核苷酸酶（CMPase）进行了超微结构水平的定位观察。结果表明:胃管状腺癌细胞腔缘微绒毛丰富,Mg²⁺—ATPase、Ca²⁺—ATPase及5NPase定位于微绒毛表面,反应明显,提示其功能代谢具有极性分布特点。粘液腺癌细胞出、入胞现象活跃,Mg²⁺—ATPase、Ca²⁺—ATPase及CMPase反应明显,认为与其粘液的大量分泌,营养物质的摄取与加工以及逃避免疫细胞的杀伤机制有关。低分化腺癌上述酶大都无反应或反应微弱。作者认为胃癌细胞的酶活性及其分布与其分化程度及功能状况有关。更多还原

【Abstract】 Ultrastructural localization of Mg²⁺-ATPase,Ca²⁺-ATPase, 5NPase and CMPase were observed in 12 cases of gastric carcinoma using electron microscopic cytochemical method. The results showed Mg²⁺-ATPase,Ca²⁺-ATPase and 5NPase are localized on the microvilli surfaces of tubular adenocarcinoma. In mucinous adenocarcinoma, Mg^2--ATPase and Ca²⁺-ATPase are localized on the outside surface of plasma membrane and extracellular secretory vesicles and the inner surface of pinosome. There are no or faint enzyme reaction products in low differentiated adenocarcinoma. The funnctional metabolism and biological character of gastric adenocarcinoma were discussed.更多还原