Carbonic anhydrase: an ultrastructural study in rat cerebellum.
The cellular and intracellular distribution of carbonic anhydrase isozyme II in rat cerebellum has been investigated with the electron microscope by the indirect antibody immunohistochemical technique. Unequivocal evidence is presented supporting the view that this enzyme is exclusively localized in oligodendrocytes. Myelin does not appear to contain detectable amounts of carbonic anhydrase though it is present in oligodendrocyte processes and in the layer of oligodendrocyte cytoplasm frequently seen to coat the external surface of myelinated fibres. The immune precipitate is found to be confined to the cytosol and the cytosolic surfaces of intracellular membranes. The data are discussed in relation to the possible function of the enzyme and the role of oligodendrocytes in the central nervous system.
D000818:Animals; D002256:Carbonic Anhydrases / Q000378:metabolism*; D002531:Cerebellum / Q000201:enzymology* / Q000648:ultrastructure; D007527:Isoenzymes / Q000378:metabolism*; D009186:Myelin Sheath / Q000201:enzymology; D009836:Oligodendroglia / Q000201:enzymology; D051381:Rats
D007527:Isoenzymes; D002256:Carbonic Anhydrases