IMMUNOHISTOCHEMICAL LOCALIZATION OF CARBONIC-ANHYDRASE ISOENZYME-II AND ISOENZYME-III IN QUAIL KIDNEY

The immunohistochemical localization of carbonic anhydrase isoenzymes has never been investigated in avian renal tissue previously. Enzyme a ctivity 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 isoenz ymes in the quail kidney. Comparison between the present findings and the corresponding histochemical patterns, previously obtained in the s ame species by a cobalt phosphate precipitation method, resulted in th e bulk of renal carbonic anhydrase activity being attributed to the ca rbonic 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 for m, antigenically distinct from the II and III isoforms, was inferred. (C) 1998 Chapman & Hall.