Carbonic anhydrase IV activity is localized on the exterior surface of human erythrocytes.
Article Details
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Wistrand PJ, Carter ND, Conroy CW, Mahieu I
Carbonic anhydrase IV activity is localized on the exterior surface of human erythrocytes.
Acta Physiol Scand. 1999 Feb;165(2):211-8. doi: 10.1046/j.1365-201x.1999.00478.x.
- PubMed ID
- 10090333 [ View in PubMed]
- Abstract
Carbonic anhydrase (CA) cytoplasmic isozymes CA I and CA II were found in human erythrocyte membrane ghosts, when prepared at pH 5.4 and pH 7.4, but not in ghosts prepared at pH 8.2. These findings could indicate that previously reported CA activity of ghosts was owing to contamination by CA I and CA II during the preparation of the ghosts. However, using a sensitive micro-assay, CA activity was also found in ghosts prepared at pH 8.2. This activity constitutes 0.2% of the erythrocytes' total CA-activity, and originates from a membrane-associated isoform of CA, located at the exterior membrane surface. It has immunochemical and kinetic properties like those of the membrane-bound CA IV, previously isolated from kidney, lung and small blood vessels. Its function is possibly to interact with the red cell membrane anionic transport protein, band 3, for the bicarbonate/chloride exchange.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Bendroflumethiazide Carbonic anhydrase 4 Protein Humans UnknownInhibitorDetails