Discrepancies between the amount of carbon dioxide eliminated from the lungs in respiration and the rate of dehydration of bicarbonate in vitro led to the discovery of carbonic anhydrase in the blood corpuscles of man and higher animals (Roughton, '35). Recently this enzyme was found to occur in the
Invertebrate red blood cell carbonic anhydrase
β Scribed by Henry, Raymond P.
- Publisher
- John Wiley and Sons
- Year
- 1987
- Tongue
- English
- Weight
- 490 KB
- Volume
- 242
- Category
- Article
- ISSN
- 0022-104X
No coin nor oath required. For personal study only.
β¦ Synopsis
This is the first report documenting the presence of carbonic anhydrase (CA) for any invertebrate red cells. CA activity was measured in plasma, hemolysates of blood cells, and in hemolymph of selected species of invertebrates. Annelid red blood cells (RBC) and sipunculid pink blood cells both possessed significant levels of CA activity. Molluscan RBC, on the other hand, lacked CA activity. The distribution appears to have fallen along phylogenetic lines, with CA being present only in blood cells of the two more closely related groups. However, the presence of extracellular CA was confirmed in oyster hemolymph. Oyster hemolymph CA showed a similar affinity (Ki) for the sulfonamide inhibitors acetazolamide and ethoxzolamide, as did the vertebrate RBC CA II isozyme, supporting the idea that this isozyme could be the ancestral form of the enzyme.
π SIMILAR VOLUMES
## Abstract Increased expression of carbonic anhydraseβrelated protein (CAβRP) VIII has previously been shown in colorectal carcinoma. Since CAβRP has no catalytic carbonic anhydrase (CA) activity, the present study attempted to elucidate its biological significance in colon cancer cells. From a co