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Journal of Experimental Biology, Vol 203, Issue 19 3003-3009, Copyright © 2000 by Company of Biologists

JOURNAL ARTICLES

Properties of a carbonic anhydrase inhibitor protein in flounder serum

T Peters, F Papadopoulos, HP Kubis and G Gros
Zentrum Physiologie, Medizinische Hochschule Hannover, Carl-Neuberg-Strasse 1, D-30623 Hannover, Germany. Peters.Thomas@mh-hannover.de.

The blood serum of the European flounder Platichthys flesus strongly inhibits soluble erythrocytic carbonic anhydrase from the same species. The inhibition is of the uncompetitive type. Hence, the mechanism of the carbonic anhydrase inhibition is different from that of all other known carbonic anhydrase inhibitors. The serum showed no inhibitory effect on carbonic anhydrase from human and bovine red blood cells. By applying the (18)O exchange reaction, it could be demonstrated that the presence of the carbonic anhydrase inhibitor in the extracellular fluid has no effect on carbonic anhydrase in intact red blood cells. Thus, this carbonic anhydrase inhibitor seems to act only within the plasma space of the circulatory system. However, the carbonic anhydrase inhibitor does appear to reduce the bicarbonate permeability of flounder red cells to approximately one-quarter of normal levels as measured by the (18)O exchange reaction. The 28 kDa carbonic anhydrase inhibitor was isolated from the serum by gel filtration. The isolated inhibitor was detected in acrylamide gels as a single band representing a 7 kDa protein. The denaturing conditions used in electrophoresis presumably led to a dissociation of the native protein into subunits.


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