منابع مشابه
Myocardial myoglobin oxygen tension.
COBURN, R. F., F. PLOEGMAKERS, P. GONDRIE, AND R. ABBOUD. Myocardial myoglobin oxygen tension. Am. J. Physiol. 224(4): 870-876. 1973.-We have applied our method of estimating mean myoglobin oxygen tension from measurements of carbon monoxide binding to myoglobin to the in vivo canine myocardium. Carbon monoxide binding to myoglobin was determined with measurements of 14C0 in myocardial biopsy s...
متن کاملIntracellular oxygen diffusion: the roles of myoglobin and lipid at cold body temperature.
Cold temperature can constrain the rate of oxygen movement through muscle cells of ectothermic animals because the kinetic energy of the solvent-solute system decreases and the viscosity of the aqueous cytoplasm increases during cooling within the physiological range of body temperatures. These factors affect the movement of both dissolved oxygen and oxymyoglobin, the two predominant routes of ...
متن کاملMyoglobin facilitated oxygen diffusion maintains mechanical function of mammalian cardiac muscle.
Myoglobin, an intracellular iron containing protein that binds oxygen reversibly, has been shown in model systems to facilitate the diffusion of oxygen and thereby maintain the mechanical function of exercising canine skeletal muscle and of hypoxic benthic fish hearts. Since no such role has yet been established for mammalian cardiac muscle small diameter (less than or equal to 0.70 mm) isolate...
متن کاملMyoglobin: Just an Oxygen Store or Also an Oxygen Transporter?
Besides acting as an oxygen store during times of reduced blood oxygen supply, myoglobin can also facilitate intracellular oxygen transport by diffusion of oxymyoglobin along a PO(2) gradient. We reassess the importance of myoglobin-facilitated oxygen diffusion by applying new findings on the intracellular diffusivity of myoglobin in a model calculation.
متن کاملMyoglobin oxygen dissociation by multiwavelength spectroscopy.
Multiwavelength optical spectroscopy was used to determine the oxygen-binding characteristics for equine myoglobin. Oxygen-binding relationships as a function of oxygen tension were determined for temperatures of 10, 25, 35, 37, and 40 degrees C, at pH 7.0. In addition, dissociation curves were determined at 37 degrees C for pH 6.5, 7.0, and 7.5. Equilibration was achieved with a myoglobin solu...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2001
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fsb2fj000497fje