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Carbonic anhydrase isozymes (CAs) are widespread zinc-containing metalloenzyme family. The enzyme catalyzes the reversible interconversion of CO2 and HCO3. This reaction is the main role of CA enzymes in physiological conditions. CA III, one of the CA isozymes, has been identified in many tissues. It is distinguished from the other isozymes by several characteristics, particularly by a lower specific activity and by its resistance to acetazolamide. However, the physiological function of CA III in fish is unknown. In this study, we examined the detection of CAs in the Shaggy sea raven Hemitripterus villosus, using SDS-PAGE, isoelectric focusing (IEF), and western blot analysis. We detected a significant protein band with molecular weight about 30 kDa from the tissues of H. villosus by SDS-PAGE and western blotting. A specific band of CA III with pI 7.0 was detected by IEF and western blotting in gill and muscle. The immunoreaction of anti-CA III expressed in the gill of H. villosus was much stronger than other tissues. One explanation for this result is that the fish gill is the only organ that is exposed to the external environment and that plays an important role in acid-base relevant ion transfer, the transfer of H and/or HCO3 , for the maintenance of systemic pH. This is the first report on the identification of a carbonic anhydrase III-like protein from H. villosus.

Presence of Carbonic Anhydrase III-like Protein in Shaggy Sea Raven, Hemitripterus villosus