Parkkila A K, Parkkila S, Juvonen T, Rajaniemi H
University of Oulu, Department of Anatomy, Finland.
Histochemistry. 1993 Jan;99(1):37-41. doi: 10.1007/BF00268018.
Human carbonic anhydrase isoenzymes I and II (HCA I and II) were purified from human erythrocytes by inhibitor affinity chromatography and ion-exchange chromatography. These isoenzymes were then located in the human adrenal gland using specific polyclonal antisera raised in rabbits and specific detection by immunohistochemical techniques. Both HCA II and I were located in the zona glomerulosa cells, although the staining for HCA I was faint. The cells of the zona fasciculata and the zona reticularis failed to stain with either antiserum. Control stainings with preimmune or anti-HCA VI sera were negative. The presence of HCA II and I in the zona glomerulosa cells may be linked to regulation of the biosynthesis or secretion of mineralocorticoids.
通过抑制剂亲和色谱法和离子交换色谱法从人红细胞中纯化出人类碳酸酐酶同工酶I和II（HCA I和II）。然后，使用在兔体内产生的特异性多克隆抗血清并通过免疫组织化学技术进行特异性检测，将这些同工酶定位在人肾上腺中。HCA II和I均位于球状带细胞中，尽管HCA I的染色较淡。束状带和网状带的细胞均未被任何一种抗血清染色。用免疫前血清或抗HCA VI血清进行的对照染色均为阴性。球状带细胞中HCA II和I的存在可能与盐皮质激素的生物合成或分泌调节有关。
