Hemoglobin–Oxygen Equilibrium Curves Measured during Enzymatic Oxygen Consumption
作者： Kim D. Vandegriff , Ronald J. Rohlfs , Michael D. Magde , Robert M. Winslow
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摘要: A rapid, new method to measure hemoglobin-oxygen equilibrium curves is described using the protocatechuic acid/protocatechuic acid 3,4-dioxygenase system [C. Bull and D.P. Ballou (1981) J. Biol. Chem. 256, 12673-12680] deoxygenate hemoglobin solutions enzymatically. The reaction followed by simultaneous measurements of spectra a diode array spectrophotometer oxygen tensions polarographic O2 microelectrode. Multicomponent analysis allows determination fractions oxyhemoglobin, deoxyhemoglobin, high-spin low-spin methemoglobins in each spectrum collected as proceeds. Fractional saturation function partial pressure calculated ratio oxyhemoglobin oxy- plus deoxyhemoglobin. Several advantages are offered this method: (i) Hemoglobin-O2 binding obtained rapidly reproducibly; (ii) speed limits methemoglobin formation autooxidation; (iii) there no gas-liquid interface, eliminating protein denaturation at surface; (iv) direct calculations fractional made spectral analysis, thus avoiding assumption linear transition between deoxy- oxyhemoglobin.
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