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Oxygen hemoglobin

Deoxyhemoglobin can bind more carbon dioxide than oxygenated hemoglobin. Therefore, unloading of oxygen in the tissues facilitates loading... [Pg.268]

Goyal, M., Azizi, F., King, S. B., Kim-Shapiro, D. B., Nitric oxide binding to oxygenated hemoglobin under physiological conditions, Biochim. Biophys. Acta 1568 (2001), p. 252-260... [Pg.104]

In addition to oxygen, hemoglobin subunits can also carry carbon dioxide. This is performed by covalent addition of C02 to the N termini of the hemoglobin chains to produce a carbonate structure. Propose reactions for this process utilizing (a) C02 and... [Pg.116]

The most important mechanism that underlies the MR appearance of ICH is the transformation of initially oxygenated hemoglobin into a series of breakdown products (deoxyhemoglobin, methemoglobin, and hemosiderin), that differ in terms of presence and number of unpaired electrons of the heme iron. Hereafter, we will discuss the influence of hemoglobin and its metabolites on T1 and T2 relaxation times. We will also briefly review the effects on MR signals of other factors such as protein concentration, clot formation and retraction, and red blood cell dehydration. [Pg.160]

Carbon monoxide is poisonous because it binds to the Fe of hemoglobin more strongly than does oxygen. Hemoglobin complexed with CO cannot carry O2 from the lungs to the tissues. Without O2 in the tissues for metabolism, cells cannot function, so they die. [Pg.1107]

Neither hemoglobin nor oxygenated hemoglobin can leave the liquid phase. Thus the fourth boundary condition states that the flux of total hemoglobin is zero. [Pg.684]

Sigmoidal E ax Model. The sigmoidal E ax model, originally derived based on oxygen-hemoglobin dissociation kinetics,is a generalization of the Emax model. It describes the response vs. drug concentration... [Pg.2803]


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See also in sourсe #XX -- [ Pg.275 ]

See also in sourсe #XX -- [ Pg.278 ]




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Binding of oxygen to myoglobin and hemoglobin

Blood oxygenator hemoglobin, oxygen binding

Blood products hemoglobin-based oxygen carriers

Encapsulated Hemoglobin as an Artificial Oxygen Carrier

Equilibrium constants hemoglobin tetramers, oxygen binding

Hemoglobin Is an Allosteric Oxygen-Binding Protein

Hemoglobin Oxygen binding

Hemoglobin and oxygen binding

Hemoglobin and oxygen transport

Hemoglobin carrying oxygen

Hemoglobin cooperative oxygen binding

Hemoglobin fetal, oxygen affinity

Hemoglobin in oxygen transport

Hemoglobin myoglobin oxygen binding

Hemoglobin oxygen affinity

Hemoglobin oxygen binding cooperativity

Hemoglobin oxygen binding curve

Hemoglobin oxygen dissociation curve

Hemoglobin oxygen release

Hemoglobin oxygen saturation

Hemoglobin oxygenated states

Hemoglobin oxygenation

Hemoglobin oxygenation

Hemoglobin oxygenation curves

Hemoglobin oxygenation, table

Hemoglobin partially oxygenated species

Hemoglobin reaction with oxygen

Hemoglobin thermodynamic function for oxygen

Hemoglobin with oxygen

Hemoglobin, abnormal human oxygenation

Hemoglobin-based oxygen carriers

Hemoglobin-based oxygen carriers HBOCs)

Hemoglobin-oxygen dissociation

Hemoglobins oxygen-linked acid groups

Oxygen affinity of hemoglobin

Oxygen binding by hemoglobin

Oxygen binding to hemoglobin

Oxygen binding, hemoglobin, calculations

Oxygen carriers, hemoglobin

Oxygen carriers, hemoglobin myoglobin

Oxygen carriers, hemoglobin synthetic

Oxygen dissociation curve of hemoglobin

Oxygen hemoglobin and

Oxygen hemoglobin, myoglobin

Oxygen in hemoglobin

Oxygen saturation curve, hemoglobin

Oxygen transport hemoglobin

Oxygen transport, by hemoglobin

Oxygen-hemoglobin dissociation kinetics

Oxygen-hemoglobin equilibrium

Oxygen-hemoglobin reaction

Oxygenation of hemoglobin

Temperature hemoglobin oxygen transport

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