oxygen affinity造句
例句与造句
- To compensate for less ambient oxygen, common ravens undergo increased respiratory rates, enhanced oxygen loading of hemoglobin at the respiratory surface, and improved oxygen affinity of hemoglobin.
- The blood of the octopus is composed of copper-rich hemocyanin which is less efficient than the iron-rich hemoglobin of vertebrates and thus does not increase oxygen affinity to the same degree.
- "H . littorale " has two types of hemoglobin, cathodic; anodic hemoglobin has a relatively low oxygen affinity and has marked Bohr effects, while cathodic hemoglobin lack significant pH effects.
- Various factors such as low pH, high CO 2 and high 2, 3 BPG at the level of the tissues favor the taut form, which has low oxygen affinity and releases oxygen in the tissues.
- The ostrich s tetramer is composed of hemoglobin type A and D, compared to typical mammalian tetramers composed of hemoglobin type A and B; hemoglobin D configuration causes a decreased oxygen affinity at the site of the respiratory surface.
- It's difficult to find oxygen affinity in a sentence. 用oxygen affinity造句挺难的
- This is due to a change in a single amino acid ( residue 143 ) found in the 2, 3-BPG'binding pocket': from histidine to serine, which gives rise to the greater oxygen affinity.
- In " H . littorale ", cathodic hemoglobin has a pronounced reversed Bohr effect in which oxygen affinity increases with decreased pH . Cathodic hemoglobin has the purpose of safeguarding oxygen transport to tissues under hypoxic and acidotic conditions.
- In addition to high P50 values, Hb Bassett shows a reduced Bohr effect ( reduced oxygen unloading ) and low cooperativity ( n = 1.4 ) resulting in lower oxygen affinity ( Abdulmalik et al ., 2004 ).
- This is further enhanced by the concomitant Bohr effect ( named after Christian Bohr, the father of Niels Bohr ), in which lowered pH ( as occurs when carbon dioxide is released in the muscles ) further lowers the oxygen affinity of hemoglobin.
- However, primitive and fetal erythrocytes, which circulate during early stages of development, are markedly different from their adult counterparts, most obviously through their larger size, shorter lifespan, nucleation, containment of different hemoglobin chains, and higher oxygen affinity.
- Further investigation and evaluation showed that unmodified cell-free haemoglobin had limitations, such as : an oxygen affinity that was too high for effective tissue oxygenation; a half-life within the intravascular space that was too short to be clinically useful; and a tendency to undergo dissociation in dimers with resultant renal tubular damage and toxicity.
- This results in the Fe 2 + ion switching to a low-spin configuration, resulting in a 20 % decrease in ionic radius so that now it can fit into the porphyrin ring, which becomes planar . ( Additionally, this hydrogen bonding results in the tilting of the oxygen molecule, resulting in a Fe O O bond angle of around 120?that avoids the formation of Fe O Fe or Fe O 2 Fe bridges that would lead to electron transfer, the oxidation of Fe 2 + to Fe 3 +, and the destruction of hemoglobin . ) This results in a movement of all the protein chains that leads to the other subunits of hemoglobin changing shape to a form with larger oxygen affinity.
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