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BioChem C785 - WGU - Module 3 Questions and answers already graded A+| Updated & Verified | 2024
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BioChem C785 - WGU - Module 3 Questions and answers already graded A+| Updated & Verified | 2024
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BioChem C785 - WGU - Module 3 Questions andanswers already graded A+| Updated & Verified |
2024
Hemoglobin's cooperative binding behavior is key to its physiological function, the binding of which
molecules influences this behavior? - ✔✔Oxygen
Carbonic anhydrase is an important enzyme present in the red blood cells that aids in efficient
transportation of carbon dioxide in the form of bicarbonate ions, from tissues to lungs. - ✔✔True
Hemoglobins ability to bind or release oxygen depends on the pH of the environment. This behavior is
known as the Bohr Effect, thus Hemoglobin binds to the oxygen at high pH and releases oxygen at a
low pH. - ✔✔True
Hemoglobin acts as a buffer and controls the pH of the blood by binding to h+ ions. - ✔✔True
In the lungs, CO2 concentration is low and the pH is high, while in the tissues, the CO2 concentration
is high and the pH is low. - ✔✔True
, In the locations where the pH is low, hemoglobin will be in the T state, allowing it to release oxygen
more effectively - ✔✔True
Increased levels of 2,3-BPG will decrease the affinity for oxygen by binding to and stabilizing the T state
of hemoglobin. The action of 2,3-BPG allows hemoglobin to release oxygen more effectively, which is
similar to the effect of low pH on the action of hemoglobin. - ✔✔True
In comparison to adult hemoglobin, fetal hemoglobin has a higher affinity for oxygen because it doesn't
bind 2,3-BPG. - ✔✔True
Myoglobin and hemoglobin each have different numbers of subunits and this affects their respective oxygen
storage and delivery capabilities. How many subunits do myoglobin and hemoglobin each have?
- ✔✔Myoglobin =
1 Hemoglobin = 4
Addition of oxygen alters the shape of the iron-heme complex, and therefore its absorption of light
as indicated by its color change from dark purple (the color of hemoglobin in venous blood) to
brilliant scarlet (the color of hemoglobin in arterial blood). - ✔✔True
Oxygen binding alters the structure of an entire hemoglobin tetramer, so the structures of
oxyhemoglobin and deoxyhemoglobin are noticeably different. The oxyhemoglobin conformation is
specifically referred to as the R (relaxed) state, whereas the deoxyhemoglobin conformation is referred
to as the T (tense) state. - ✔✔True
Patients with sickle cell anemia have atypical hemoglobin, which will distort the red blood cells into
sickle shape during oxygen delivery. The substitution of a hydrophilic amino acid with a hydrophobic
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