Kondo T, Taniguchi N, Hirano T, Kawakami Y
J Biol Chem. 1984 Dec 25;259(24):15517-22.
A low-activity form of erythrocyte carbonic anhydrase isozyme I was found in patients with primary aldosteronism. The specific activity was very low, but the activity was restored by drug treatment as well as adrenalectomy. The enzyme was purified to homogeneity from one of the patients. With respect to its antigenicity and zinc content, the low-activity form was not distinguishable from the normal enzyme. On the other hand, the inhibition constant and binding affinity to acetazolamide of the low-activity enzyme were lower than those of normal enzyme. Sulfhydryl group titration, amino acid analysis, and peptide-mapping analysis suggested that the low-activity enzyme contains a mixed disulfide with glutathione which is closely associated with its low activity.
在原发性醛固酮增多症患者中发现了一种低活性形式的红细胞碳酸酐酶同工酶I。其比活性非常低，但通过药物治疗和肾上腺切除术后活性得以恢复。从其中一名患者身上将该酶纯化至同质。就其抗原性和锌含量而言，低活性形式与正常酶无法区分。另一方面，低活性酶对乙酰唑胺的抑制常数和结合亲和力低于正常酶。巯基滴定、氨基酸分析和肽图谱分析表明，低活性酶含有与谷胱甘肽形成的混合二硫键，这与其低活性密切相关。
