Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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Describe the structure of hemoglobin and How does the structure of hemoglobin allow it to combine
with oxygen?
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- The muscles of deep diving mammals such as whales contain exceptionally large amounts ofmyoglobin. How does this circumstance contribute to prolonged dives?arrow_forwardIn our discussion of oxygen binding, we saw how oxygen affinity may be affected by temperature. The book mentions that "temperature effects may become a problem in the hypothermic limbs of mammals in Arctic climates," (pg. 650) but it doesn't explain why. Given what you understand about oxygen binding affinity and temperature, why would these animals have an issue? O The cold temperatures increase the binding affinity of oxygen to myoglobin. The cold temepratures decrease the binding affinity of oxygen to hemoglobin. The cold temperatures increase the binding affinity of oxygen to hemoglobin. The cold temperatures decrease the bindingg affinity of oxygen to myoglobin.arrow_forwardWhat is in hemoglobin that brings oxygen to the different parts of the body?arrow_forward
- What other diseases are associated with estraneous forms of hemoglobin subunits in the human adult?arrow_forwardWhich of the following statements is correct of BOTH haemoglobin and myoglobin? Acidic conditions increase the affinity for oxygen. The iron atom of the heme prosthetic group is bound to nitrogen atoms at five of six coordination sites. Four oxygen molecules bind to each subunit. Quaternary structure is found in both haemoglobin and myoglobin. Both haemoglobin and myoglobin show the same oxygen binding affinity at differentarrow_forwardThe O2-binding curve for Hemoglobin (Hb) is sigmoidal because: a O2 binding to Hb increases the binding affinity of Hb for additional O2. b The pH of blood is near the pKa of histidine. c The pH of the bloodstream changes with changes in O2 concentration. d Hb’s O2-binding affinity changes with changes in pH.arrow_forward
- When oxygenated blood (Hemoglobin nearly 100% saturated), reaches resting systemic tissues, what percentage of the available oxygen is unloaded from hemoglobin? 100%, 75%, 50%, or 25%?arrow_forwardRecall from your BI110 class that metabolically active tissues produce CO2 as a by-product of cellular respiration. Those metabolically active tissues require the O2 that is brought by hemoglobin for the same process (cellular respiration). Explain why the effect of pH on hemoglobin’s affinity for oxygen is consistent with delivering it to actively metabolizing tissues. (Hint: think about what effect the presence of CO2 has on the tissues…)arrow_forwardWhat effect would hyperventilation (rapid breathing) have on the concentration of oxyhemoglobin in the bloodstream?arrow_forward
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