Gabrielli M G, Vincenzetti S, Vita A, Menghi G
Department of Molecular, Cellular and Animal Biology, University of Camerino, Italy.
Histochem J. 1998 Jul;30(7):489-97. doi: 10.1023/a:1003295420218.
The immunohistochemical localization of carbonic anhydrase isoenzymes has never been investigated in avian renal tissue previously. Enzyme activity has largely been documented by histochemical and physiological reports. In this investigation, specific antisera were used to study the distribution of the cytosolic carbonic anhydrase II and III isoenzymes in the quail kidney. Comparison between the present findings and the corresponding histochemical patterns, previously obtained in the same species by a cobalt phosphate precipitation method, resulted in the bulk of renal carbonic anhydrase activity being attributed to the carbonic anhydrase II isoenzyme. Conversely, moderate carbonic anhydrase III immunostaining appeared to be confined to the smooth muscle cells of ureteral and arteriolar walls. Indirect evidence of the occurrence, in the quail kidney, of a membrane-associated carbonic anhydrase form, antigenically distinct from the II and III isoforms, was inferred.
此前从未有人对鸟类肾脏组织中碳酸酐酶同工酶的免疫组化定位进行过研究。酶活性主要通过组织化学和生理学报告得以记录。在本研究中，使用特异性抗血清来研究鹌鹑肾脏中胞质碳酸酐酶II和III同工酶的分布。将本研究结果与之前用磷酸钴沉淀法在同一物种中获得的相应组织化学模式进行比较，结果表明，大部分肾脏碳酸酐酶活性归因于碳酸酐酶II同工酶。相反，中等强度的碳酸酐酶III免疫染色似乎局限于输尿管和小动脉壁的平滑肌细胞。由此推断，鹌鹑肾脏中存在一种与膜相关的碳酸酐酶形式，其抗原性与II型和III型同工酶不同，这是间接证据。
