Fig. 4. Oxygen-binding characteristics and isoHb differentiation of crucian carp
Hb, measured in the presence of 0.1 mol l-1 KCl and 0.1 mol
l-1 Hepes buffers. (A) Oxygen tensions and Hill's cooperativity
coefficients at 50% saturation (P50 and n50 of stripped
hemolysates and their pH dependence (Bohr plots) at 10°C (
) and
20°C (
) and of the lysate in the presence of saturating concentration
of ATP (ATP/tetrameric Hb ratio, 9.6), (
), [haem], 0.50 mmol
l-1. (B) Oxygen equilibrium curves at 10°C, 20°C and
20°C in the presence of saturating ATP (interpolated from data in A). (C)
Isoelectric focusing profile, showing absorptions at 540 nm () and pH
values at 25°C (
) of eluted fractions, and the presence of three
major (II, III and IV) and two minor (I and V) isoHbs. (D) Bohr plots of
isoHbs I-IV, at 10 and 20°C.