Proteolytic cleavage of band 3 protein in relation to anion transport in fish (Oncorhynchus mykiss) red blood cells |
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Institution: | 1. Faculty of Food Science and Nutrition, School of Health Sciences, University of Iceland. University of Iceland, Sæmundargata 2, 101 Reykjavik, Iceland;2. Zymetech, Fiskislod 39, 101 Reykjavík, Iceland |
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Abstract: | - 1.1. The effects of trypsin and chymotrypsin on HCO3?/Cl? exchange through red blood cell membranes of humans and trout were studied.
- 2.2. To measure the anion exchange we used a right-angle light-scattering technique by applying the Jacobs-Stewart cycle in ammonium solution and the osmotiration method at constant cell volume.
- 3.3. The Cl? flux in human red blood cells remained unaltered after treatment with external trypsin and chymotrypsin while in trout red blood cells the flux decreased.
- 4.4. This partial inhibition of anion transport in fish, ranging from 30 to 40%,suggest that one or several of the cleavage sites in band 3 protein, essential for anion transport function, are exposed in fish red blood cells.
- 5.5. In human red blood cells the fragments of band 3 which are affected by proteolytic digestion, retain their tertiary structure because there is no influence on anion transport.
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