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Myoglobin function reassessed

Jonathan B. Wittenberg^* and Beatrice A. Wittenberg

Department of Physiology and Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA

View larger version (19K): [in a new window]   Fig. 1. Relation of myoglobin concentration in muscles of various animals to their cytochrome oxidase activity. Modified from Lawrie (1953).

View larger version (135K): [in a new window]   Fig. 2. (A) portion of a myocyte from the ventricular papillary muscle of the cat. Reproduced with permission from Fawcett (1966). (B) A portion of a modified striated muscle cell from the heater organ of the eye of the blue marlin. Reproduced with permission from Block and Franzini-Armstrong (1988).

View larger version (17K): [in a new window]   Fig. 3. (A) Steady-state oxygen uptake of suspensions of cardiac myocytes as functions of carbon monoxide partial pressure. Oxygen uptake is normalized, taking the uninhibited rate in each experiment as unity. Oxygen partial pressure (PO2) is equal to 10.6–12.0 kPa (80–90 torr) or 13.3–16.0 kPa (100–120 torr). The oxymyoglobin-dependent portion of the oxygen uptake is taken as the difference between the uninhibited rate and the plateau value at high carbon monoxide partial pressure (PCO). Carbon monoxide inhibition of cytochrome oxidase becomes evident above PCO=80 kPa (600 torr). Reproduced from Wittenberg and Wittenberg (1987). (B) Oxymyoglobin-dependent oxygen uptake of suspensions of cardiac myocytes as functions of mole fraction carbon monoxide myoglobin (MbCO). Since myoglobin (Mb) is essentially fully occupied by ligands, mole fraction MbO2 = 1 –mole fraction MbCO. In different experiments, PO2 is equal to 5.3–8.0 kPa (40–60 torr), 9.3–12.0 kPa (70–90 torr), 13.3–16.0 kPa (100–120 torr) or 45 kPa (340 torr). Reproduced from Wittenberg and Wittenberg (1987).

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