Electrolyte Composition of Mink (Mustela vison) Erythrocytes and Active Cation Transporters of the Cell Membrane.docVIP

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Electrolyte Composition of Mink (Mustela vison) Erythrocytes and Active Cation Transporters of the Cell Membrane.doc

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Electrolyte Composition of Mink (Mustela vison) Erythrocytes and Active Cation Transporters of the Cell Membrane

Acta vet. scand. 2001, 42, 261-270. Electrolyte Composition of Mink (Mustela vison) Erythrocytes and Active Cation Transporters of the Cell Membrane By O. Hansen and T. N. Clausen Department of Physiology, Aarhus University, ?rhus, and Danish Fur Breeders Research Centre, Tvis, Holste- bro, Denmark. Hansen O, Clausen TN: Electrolyte composition of mink (Mustela vison) erythro- cytes and active cation transporters of the cell membrane. Acta vet. scand. 2001, 42, 261-270. – Red blood cells from mink (Mustela vison) were characterized with re- spect to their electrolyte content and their cell membranes with respect to enzymatic ac- tivity for cation transport. The intra- and extracellular concentrations of Na+, K+, Cl-, Ca2+ and Mg2+ were determined in erythrocytes and plasma, respectively. Plasma and red cell water content was determined, and molal electrolyte concentrations were calcu- lated. Red cells from male adult mink appeared to be of the low-K+, high-Na+ type as seen in other carnivorous species. The intracellular K+ concentration is slightly higher than the extracellular one and the plasma-to-cell chemical gradient for Na+ is weak, though even the molal concentrations may differ signi?cantly. Consistent with the high intracellular Na+ and low K+ concentrations, a very low or no ouabain-sensitive Na+,K+- ATPase activity and no K+-activated pNPPase activity were found in the plasma mem- brane fraction from red cells. The Cl- and Mg2+ concentrations expressed per liter cell water were signi?cantly higher in red cells than in plasma whereas the opposite was the case with Ca2+. The distribution of Cl- thus does not seem compatible with an inside- negative membrane potential in mink erythrocytes. In spite of a steep calcium gradient across the red cell membrane, neither a calmodulin-activated Ca2+-ATPase activity nor an ATP-activated Ca2+-pNPPase activity were detectable in the plasma membrane frac- tion. The origin of a supposed primary