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Water regulates oxygen binding in hagfish (Myxine glutinosa) hemoglobin

Gabriele Müller, Angela Fago^* and Roy E. Weber

Department of Zoophysiology, Institute of Biology, Building 131, University of Aarhus, DK-8000 Aarhus C, Denmark

View larger version (28K): [in a new window]   Fig. 1. Relative change in P50 as a function of water activity logeaw in stripped hemolysate (A,B) and in equimolar hemoglobin mixtures of HbI and HbII (HbI+II; C,D) and HbII and HbIII (HbII+III; E,F) in the absence (A,C,E) and presence (B,D,F) of CO2, and the presence of glycine (filled circles) or glucose (open circles). For regression coefficients, see Table 1.

View larger version (24K): [in a new window]   Fig. 2. Relative change in P50 as a function of solution osmolality (logeOsm) in stripped hemolysate (A,B) and in equimolar hemoglobin mixtures of HbI and HbII (HbI+II; C,D) and HbII and HbIII (HbII+III; E,F) in the absence (A,C,E) and presence (B,D,F) of CO2, and the presence of glycine (filled circles) or glucose (open circles). For regression coefficients, see Table 1.

View larger version (27K): [in a new window]   Fig. 3. Oxygen equilibrium curves for intact red blood cells equilibrated at various osmolalities (0.25-1.0 osmol kg-1). Inset, Hill plots of the data. Values are means ± S.E.M. obtained from fitting the observed spectra.

View larger version (20K): [in a new window]   Fig. 4. Effect of solution water activity on the relative change in P50 in red blood cells (RBC) (Fig. 3) (grey circles) and in stripped hemolysate (Fig. 1) with added glycine (filled symbols) or glucose (open symbols) in the absence (circles) and presence (triangles) of CO2.