Briggman J V, Tashian R E, Spicer S S
Am J Pathol. 1983 Sep;112(3):250-7.
Isozymes of carbonic anhydrase (CA) were localized immunohistochemically by the immunoglobulin-peroxidase bridge technique on fixed paraffin sections of human eccrine sweat glands. Low-activity CA I was identified in the cytoplasm of the myoepithelial cells in the secretory coil and in the luminal and basal cells of both the coiled and straight segments of the duct. High-activity CA II was found in the cytoplasm of clear cells of the secretory coil. Although evidence has suggested that CA activity is altered in cystic fibrosis (CF), the present immunohistochemical comparison of CF sweat glands revealed a distribution of and, semiquantitatively, a prevalence of CA isozymes identical to those of normal sweat glands. Abnormal enzyme activity cannot be ruled out, however, on the basis of immunocytochemical staining which depends solely on the antigenic properties of CA.
采用免疫球蛋白-过氧化物酶桥技术，对人外泌汗腺固定石蜡切片进行免疫组织化学定位碳酸酐酶（CA）同工酶。在分泌盘曲部肌上皮细胞的细胞质以及导管盘曲段和直段的管腔细胞及基底细胞中，鉴定出低活性的CA I。在分泌盘曲部透明细胞的细胞质中发现高活性的CA II。尽管有证据表明囊性纤维化（CF）患者的CA活性发生改变，但目前对CF汗腺的免疫组织化学比较显示，CA同工酶的分布以及半定量的患病率与正常汗腺相同。然而，基于仅依赖CA抗原特性的免疫细胞化学染色，不能排除酶活性异常的情况。
