O'Brien P, Rosen S, Trencis-Buck L, Silen W
Gastroenterology. 1977 May;72(5 Pt 1):870-80.
Bullfrog fundic mucosa was separated into fractions containing predominantly surface epithelial cells, mucous neck cells, and and oxyntic cells, respectively, and the carbonic anhydrase concentration of each fraction and of antral mucosa was measured. There were no significant differences between the enzyme concentrations of these fractions. The mean level was 12.4 units of activity per milligram of protein. The cellular localization of carbonic anhydrase in the gastric fundic and antral mucosa of the bullfrog, rat, rabbit, and dog was studied using a specific histochemical technique. The enzyme was shown to be present in both parietal and nonparietal epithelium of all species and to characterize a specific cell type in the dog antrum. The widespread distribution of high levels of carbonic anhydrase activity in both acid secreting and nonsecreting cells of the gastric mucosa suggests a possible role for the enzyme beyond one solely relating to acid secretion.
牛蛙胃底黏膜被分别分离成主要含有表面上皮细胞、黏液颈细胞和壁细胞的组分,并测定了每个组分以及胃窦黏膜中碳酸酐酶的浓度。这些组分的酶浓度之间没有显著差异。平均水平为每毫克蛋白质12.4个活性单位。使用特定的组织化学技术研究了牛蛙、大鼠、兔子和狗的胃底和胃窦黏膜中碳酸酐酶的细胞定位。结果表明,该酶存在于所有物种的壁细胞和非壁细胞上皮中,并且在犬胃窦中表征一种特定的细胞类型。胃黏膜中酸分泌细胞和非分泌细胞中高水平碳酸酐酶活性的广泛分布表明,该酶的作用可能不仅仅与酸分泌有关。