Concept explainers
To describe:
The effect of iron deficiency in humans which is responsible for carrying oxygen in red blood cells.
Introduction:
Trace elements or minerals are those elements that are required by the body of an organism in small amount. These include iron, manganese, copper, molybdenum, zinc, boron, chlorine, nickel, iodine, selenium, chromium, silicon, vanadium, fluoride, lead cadmium, mercury, arsenic, aluminum. They are present in small amount but are important for the growth and development of body.
Some of these trace elements are used as a catalyst for enzymatic reactions. Trace elements are toxic if it is consumed in higher quantity. Trace elements are of two types essential and non essential. Essential trace elements are those which are required for the growth and development while non essential elements are those that are present in the body but are not required for growth and development.
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CAMPBELL BIOLOGY IN FOCUS-TEXT,AP ED.
- A molecule of hemoglobin ________. is shaped like a biconcave disk packed almost entirely with iron contains four glycoprotein units studded with oxygen consists of four globin proteins, each bound to a molecule of heme can carry up to 120 molecules of oxygenarrow_forward2. j The following plots show an oxygen binding curve for hemoglobin under a certain set of conditions. For each plot, sketch (with reasonable accuracy) a second curve showing how the binding of oxygen to hemoglobin would be altered by the change in conditions noted. a. Increase in pCO2 b. Dissociation of native Hb into aß dimers 1 0.8 0.8 0.6 Y 0.4 0.6 Y 0.4 0.2 0.2 po2 pO2arrow_forward7L.3arrow_forward
- Watch this video (http://openstaxcollege.org/l/oxyblood) to see the transport of oxygen from the lungs to the tissues. Why is oxygenated blood bright red, whereas deoxygenated blood tends to be more of a purple color?arrow_forward3. When muscles are more active physiological conditions change to affect oxygen binding to Hemoglobin. Briefly describe the changes that occur and why this affects hemoglobin function. Draw the shifted curve on the graph above. A. What physiological conditions change during exercise (levels of what molecules are increasing/decreasing)? B. How do these molecules directly affect Hb’s structure ? What interactions does this stabilize ? C. How do these interactions affect the affinity of Hb for O2? How would this affect the binding curve for Hb? Draw on the graph provided. D. How will this shift in the binding curve affect the function of Hemoglobin ? E.Where does the physiological pO2 in the tissues fall on the O2 binding curve ? In the lungs ? Why is this physiologically important?arrow_forward2 When an oxygen molecule binds to the deoxyhemoglobin, multiple conformational changes happen that switch the hemoglobin from a T state to an R state. Describe the key conformational changes that happen that lead to the switch of Hemoblogin to an R state, starting with oxygen binding.arrow_forward
- Part C - Exploring the cooperative binding of oxygen Oxygen shows cooperative binding to hemoglobin. Cooperative binding has the following effects on the binding and release of oxygen: Oxygen binding to hemoglobin: When one molecule of oxygen binds to one of hemoglobin's four subunits, the other subunits change shape slightly, increasing their affinity for oxygen. Oxygen release from hemoglobin: When four oxygen molecules are bound to hemoglobin's subunits and one subunit releases its oxygen, the other three subunits change shape again. This causes them to release their oxygen more readily. These two graphs show how cooperative binding differs from a hypothetical situation where binding is not cooperative. • The x-axis shows the partial pressure of oxygen (PO₂). This is a measure of the amount of oxygen present in a tissue. The blue arrows on the x-axis show the partial pressure of oxygen in various tissues of the body. • The y-axis shows the oxygen saturation of hemoglobin (O₂…arrow_forwardSolve all asaparrow_forwardWhich of the following factors play a role in the oxygen-hemoglobin saturation, dissociation curve? temperature pH BPG all of the abovearrow_forward
- #4arrow_forward30. The cooperative binding behavior of hemoglobin for oxygen is best explained by... Group of answer choices The movement of the proximal histidine upon O2 binding causes a structural change at the binding interface between subunits The oxidation of Fe2+ to Fe3+ and formation of the superoxide ion causes distortion of the protoporphyrin ring, altering binding interface between subunits The tetrameric nature of hemoglobin's quaternary structure directly confers cooperative binding activity The movement of the distal histidine upon O2 binding causes a structural change at the binding interface between subunits The binding of O2 causes a pH shift that changes the protonation state of amino acids located at the interface between subunits The solubility of hemoglobin in aqueous solution and its insolubility in nonpolar environmentsarrow_forwardWHAT IF? A doctor might give bicarbonate (HCO3-) to apatient who is breathing very rapidly. What is the doctorassuming about the patient’s blood chemistry?arrow_forward
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