title: Immunohistochemical localization of carbonic anhydrase isoenzymes II and III in quail kidney.
abstract: The immunohistochemical localization of carbonic anhydrase isoenzymes has never been investigated in avian renal tissue previously. Enzyme activity has largely been documented by histochemical and physiological reports. In this investigation, specific antisera were used to study the distribution of the cytosolic carbonic anhydrase II and III isoenzymes in the quail kidney. Comparison between the present findings and the corresponding histochemical patterns, previously obtained in the same species by a cobalt phosphate precipitation method, resulted in the bulk of renal carbonic anhydrase activity being attributed to the carbonic anhydrase II isoenzyme. Conversely, moderate carbonic anhydrase III immunostaining appeared to be confined to the smooth muscle cells of ureteral and arteriolar walls. Indirect evidence of the occurrence, in the quail kidney, of a membrane-associated carbonic anhydrase form, antigenically distinct from the II and III isoforms, was inferred.
authors: Department of Molecular, Cellular and Animal Biology, University of Camerino, Italy.
authors: M G
authors: MG
authors: Gabrielli
authors: S
authors: S
authors: Vincenzetti
authors: A
authors: A
authors: Vita
authors: G
authors: G
authors: Menghi
mesh_terms: D000818:Animals; D001160:Arterioles / Q000201:enzymology; D015153:Blotting, Western; D002256:Carbonic Anhydrases / Q000378:metabolism*; D003370:Coturnix; D007150:Immunohistochemistry; D007668:Kidney / Q000201:enzymology*; D007678:Kidney Glomerulus / Q000201:enzymology; D007686:Kidney Tubules, Distal / Q000201:enzymology; D007687:Kidney Tubules, Proximal / Q000201:enzymology; D009130:Muscle, Smooth / Q000201:enzymology / Q000378:metabolism; D014513:Ureter / Q000201:enzymology
chemical_list: D002256:Carbonic Anhydrases