Wachsmuth E D, Thöner M, Pfleiderer G
Histochemistry. 1975 Nov 21;45(2):143-61. doi: 10.1007/BF00495158.
The use of the immuno-histochemical method permits the localization of aldolase isozymes in tissue sections. Upon incubating a section with a monomer-specific antiserum, isozymes containing that monomer remain in the section, whereas other cytoplasmic enzymes diffuse out of the section. If soluble antigen is added subsequently, it is bound by the tissue-bound antibody. These antibody fixed aldolases can then be stained by the use of a tetrazolium test linked to substrate hydrolysis. In this way it was demonstrated that isozymes of aldolase containing mostly the A monomer are predominantly localized in the distal tubules, the collecting tubules, the vessels and capillaries of the kidney, the ganglia, the Purkinje cells, the neurons, the white matter and the chorioid plexus of the brain. Aldolase containing mostly B-monomers were found in the proximal tubules. Aldolase isozymes particularly rich in C-monomers were seen in the nervus opticus, the pia mater, the vessels of cerebrum and the molecular layer of the cortex cerebelli.
免疫组织化学方法的应用能够在组织切片中定位醛缩酶同工酶。用单体特异性抗血清孵育切片时,含有该单体的同工酶会保留在切片中,而其他细胞质酶则会扩散出切片。如果随后加入可溶性抗原,它会与组织结合的抗体结合。然后可以通过与底物水解相关的四氮唑试验对这些抗体固定的醛缩酶进行染色。通过这种方式证明,主要含有A单体的醛缩酶同工酶主要定位于远端小管、集合小管、肾脏的血管和毛细血管、神经节、浦肯野细胞、神经元、白质以及脑脉络丛。在近端小管中发现主要含有B单体的醛缩酶。在视神经、软脑膜、大脑血管和小脑皮质分子层中可见特别富含C单体的醛缩酶同工酶。