Laursen A B, Klauber A, Jensen O A
Acta Ophthalmol (Copenh). 1980 Aug;58(4):496-506. doi: 10.1111/j.1755-3768.1980.tb08290.x.
Location and in vitro determination of Na-K ATP'ase activity in the anterior structures of individual human lenses with senile cataract are reported, with special reference to anterior capsular/subcapsular opacity (ACSCO). Histochemically, ATP'ase reaction products were found exclusively in the epithelium. Even totally opaque lenses showed strong positive reactions. Biochemically, increasing ratios of Na+/K+ concentrations in the assay medium resulted in an increase in enzyme activity to a limited degree, whereafter the activity remained stable. We cannot decide whether the Na-K ATP'ase activity of the anterior lens structures is unchanged in relation to ACSCO as indicated by our figures. For there are methodological problems, although our analytical error, expressed as the variation coefficient for slaughterhouse pig lenses, seems to be one of the lowest so far reported in the literature on interindividual, non-pooled material.
报告了在患有老年性白内障的个体人晶状体前部结构中钠钾ATP酶活性的定位及体外测定结果,特别提及前囊膜/囊下混浊(ACSCO)。组织化学上,ATP酶反应产物仅在上皮细胞中发现。即使是完全混浊的晶状体也显示出强烈的阳性反应。生物化学方面,测定介质中Na⁺/K⁺浓度比值增加会使酶活性在一定程度上增加,之后活性保持稳定。根据我们的数据,我们无法确定晶状体前部结构的钠钾ATP酶活性相对于ACSCO是否未发生变化。因为存在方法学问题,尽管以屠宰场猪晶状体的变异系数表示的分析误差似乎是目前文献中报道的关于个体间、非混合材料的最低误差之一。