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| Quaternary structure of Hemoglobin |
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Definition
| 2 pairs of unlike polypeptide chains (2 alpha and 2 nonalpha) linked by salt binds, hydrophobic contacts, and hydrogen bonds |
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| heme is a non protein portion of hemoglobin, the porphyrin ring contains iron in the hydrophobic crevasse (4 rings/molecule) |
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| alpha, beta, delta and gamma arranged in identical pairs composed of two different chains |
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| HbF: two alpha and two gamma chains |
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| HbA: two alpha and two beta chains |
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| pH, temperature, 2,3-BPG and CO2 and oxygen dissociation curves |
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Definition
| Increase, shift right, decrease oxygen affinity. Decrease, shift left, increase oxygen affinity |
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| Hemoglobins Function in gaseous transport |
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Definition
| Hemoglobin functions to bind oxygen and carry it to different tissues. The dissociation and association of oxygen to hemoglobin depends on the partial pressure in it's environment, when the pressure it high, hemoglobin releases oxygen and when it's low, hemoglobin holds onto oxygen |
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Definition
15.0g/dL for adults and
17.0g/dL for an infant |
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| Maintenance of Hemoglobin concentration |
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Definition
| activity of (1)ALAS2 (2) PBGD (3) iron concentration and (4) regulation of globin chain synthesis |
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Definition
| major hemoglobin (2 alpha and 2 beta chains), reaches 95% by age 1 |
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| glycosylated hemoglobin, produced depending on glucose concentration, older RBCs have more HbA1c, used as an indicator of glucose levels in diabetics |
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Definition
| iron is either pooled for metabolic processes or stored. Globin synthesis is activated by heme which inactivates transcription inhibitor. |
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Definition
| HbF has greater affinity for oxygen than HbA. HbF has two alpha and two gamma chains while HbA has two alpha and two beta chains |
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Definition
| oxyhemoglobin, salt bridges are broken, high oxygen affininty, 2,3-BPG is expelled, pulls beta chains together while loading oxygen |
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| deoxyhemoglobin, stabilzed by salt bridges, low oxygen affinity, 2,3-BPG is bound, allosteric effectors |
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| abnormal hemoglobin is aquired by... |
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Definition
| exposure to oxidizing chemicals (methemoglobin) exposure to sulfur compounds, pollution or drugs (sulfhemoglobin) or exposure to city air or smoke (carboxyhemoglobin) |
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Term
| Detect methmeoglobin by... |
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Definition
| demonstration of maximum absorbace band at 630nm in pH 7.0 via blood sample (brown) |
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Definition
| Hemogobin with iron in ferric state, cannot bind oxygen and decreases the oxygen carrying capacity of the blood |
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| sulfur atom binds to periphery of prophyrin ring of the heme group, and heme groups become ineffective for oxygen transport |
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| detect carboxyhemoglobin... |
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Definition
| absorption band at 541nm, cherry red color of blood |
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Definition
| hemoglobin is exposed to CO, which has it has a higher affinity for, irreversibly bound |
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| oxygen affinity of methemoglobin |
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Definition
| increases oxygen affinity in remaining normal hemoglobin because it cannot bind hemoglobin |
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| oxygen affinity of sulfhemoglobin |
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Definition
| decreases oxygen affinity of hemoglobin |
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Term
| oxygen affinity of carboxyhemoglobin |
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Definition
| increase oxygen affinity in remaining hemoglobin and a decrease in release of oxygen by already bound hemoglobin, CO takes up the oxygen binding position |
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Term
| Exchange of CO2 in the lungs and capillaries |
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Definition
| CO2 moves from the high pressure in the capillaries to low pressure in the lungs in order to be expelled |
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Term
| exchange of O2 in the lungs and capillaries |
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Definition
| O2 moves from the high pressure in the lungs to the low pressure in the capillaries where it is bound by hemoglobin and moved to the tissues |
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Term
| exchange of H+ in lungs and capillaries |
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Definition
| H+ binds to deoxyhemoglobin (T state)increases affinity for CO2 |
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Definition
| effect of pH on hemoglobin-oxygen affinity. This is one of the most important buffer systems in the body. As the H+ concentration in tissues increases, the affinity of hemoglobin for oxygen is decreased, permitting the unloading of oxygen |
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Definition
| phenomenon in which a plasma CI- diffuses into the erythrocyte when a free bicarbonate iron diffuses out of the erythrocyte |
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| bluish color of the skin and mucous membrane that develops as a result of excess deoxygenated hemoglobin in the blood |
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| hemoglobin that has glucose irreversibly attached to the terminal amino acid of the beta chains. Also called HbA1c |
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| deficiency of oxygen to the cells |
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| Iron regulatory protein (IRP) |
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Definition
| protein that binds to a stem-loop structure of ferritin and transferrin receptor mRNA. The stem-loop structure of mRNA is known as IRE-BP. The binding affinity of IRE-BP for the IRE is determined by the amount of cellular iron. The IRE-BP is involved in the regulation of transferring receptors and ferritin |
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