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Essentials of the Living World 5th Edition by George Johnson
Edition 5ISBN: 978-0078096945Essentials of the Living World 5th Edition by George Johnson
Edition 5ISBN: 978-0078096945 Exercise 3
How Does pH Affect a Protein's Function?
The red blood cells you see to the lower right carry oxygen to all parts of your body. These cells are red because they are chock-full of a large iron-rich protein called hemoglobin. The iron atoms in each hemoglobin molecule provide a place for oxygen gas molecules to stick to the protein. When oxygen levels are highest (in the lungs), oxygen atoms bind to hemoglobin tightly, and a large percentage of the hemoglobin molecules in a cell possess bound oxygen atoms. When oxygen levels are lower (in the tissues of the body), hemoglobin doesn't bind oxygen atoms as tightly, and as a consequence hemoglobin releases its oxygen to the tissues. What causes this difference between lungs and tissues in how hemoglobin loads and unloads oxygen? Oxygen concentration is not the only factor that might be responsible. A protein's function canbe affected by pH, and blood pH, for example, also differs between lungs and body tissues ( pH is a measure of how many H + ions a solution contains). Tissues are slightly more acidic (that is, they have more H + ions and a lower pH). Their metabolic activities release CO 2 into the blood, which quickly becomes converted to carbonic acid and lowers the pH.
The graph to the right displays so-called "oxygen loading curves" that reveal the effectiveness with which hemoglobin binds oxygen. The more effective the binding, the less oxygen required before hemoglobin becomes fully loaded and the farther to the left a loading curve is shifted. To assess the impact of pH on this process, O 2 loading curves were carried out at three different blood pH values. In the graph, oxygen levels in the blood are presented on the x axis, and for each data point the corresponding % hemoglobin saturation ( %, or percent, is the numerator [top part] of a fraction whose denominator [bottom part] is 100-in this case, a measure of the fraction of the hemoglobin that is bound to oxygen) is presented on the y axis. The oxygen-loading curve was repeated at pH values of 7.6, 7.4, and 7.2, corresponding to the blood pH that might be expected in resting, exercising, and very active muscle tissue, respectively.![How Does pH Affect a Protein's Function? The red blood cells you see to the lower right carry oxygen to all parts of your body. These cells are red because they are chock-full of a large iron-rich protein called hemoglobin. The iron atoms in each hemoglobin molecule provide a place for oxygen gas molecules to stick to the protein. When oxygen levels are highest (in the lungs), oxygen atoms bind to hemoglobin tightly, and a large percentage of the hemoglobin molecules in a cell possess bound oxygen atoms. When oxygen levels are lower (in the tissues of the body), hemoglobin doesn't bind oxygen atoms as tightly, and as a consequence hemoglobin releases its oxygen to the tissues. What causes this difference between lungs and tissues in how hemoglobin loads and unloads oxygen? Oxygen concentration is not the only factor that might be responsible. A protein's function canbe affected by pH, and blood pH, for example, also differs between lungs and body tissues ( pH is a measure of how many H + ions a solution contains). Tissues are slightly more acidic (that is, they have more H + ions and a lower pH). Their metabolic activities release CO 2 into the blood, which quickly becomes converted to carbonic acid and lowers the pH. The graph to the right displays so-called oxygen loading curves that reveal the effectiveness with which hemoglobin binds oxygen. The more effective the binding, the less oxygen required before hemoglobin becomes fully loaded and the farther to the left a loading curve is shifted. To assess the impact of pH on this process, O 2 loading curves were carried out at three different blood pH values. In the graph, oxygen levels in the blood are presented on the x axis, and for each data point the corresponding % hemoglobin saturation ( %, or percent, is the numerator [top part] of a fraction whose denominator [bottom part] is 100-in this case, a measure of the fraction of the hemoglobin that is bound to oxygen) is presented on the y axis. The oxygen-loading curve was repeated at pH values of 7.6, 7.4, and 7.2, corresponding to the blood pH that might be expected in resting, exercising, and very active muscle tissue, respectively. Making Inferences At an oxygen level of 40 mm H g , would hemoglobin bind oxygen more tightly at a pH of 7.8 or 7.0?](https://d2lvgg3v3hfg70.cloudfront.net/SM1254/11eb5a3b_7ba2_8210_a349_c7ac20659254_SM1254_00.jpg)
Making Inferences At an oxygen level of 40 mm H g , would hemoglobin bind oxygen more tightly at a pH of 7.8 or 7.0?
The red blood cells you see to the lower right carry oxygen to all parts of your body. These cells are red because they are chock-full of a large iron-rich protein called hemoglobin. The iron atoms in each hemoglobin molecule provide a place for oxygen gas molecules to stick to the protein. When oxygen levels are highest (in the lungs), oxygen atoms bind to hemoglobin tightly, and a large percentage of the hemoglobin molecules in a cell possess bound oxygen atoms. When oxygen levels are lower (in the tissues of the body), hemoglobin doesn't bind oxygen atoms as tightly, and as a consequence hemoglobin releases its oxygen to the tissues. What causes this difference between lungs and tissues in how hemoglobin loads and unloads oxygen? Oxygen concentration is not the only factor that might be responsible. A protein's function canbe affected by pH, and blood pH, for example, also differs between lungs and body tissues ( pH is a measure of how many H + ions a solution contains). Tissues are slightly more acidic (that is, they have more H + ions and a lower pH). Their metabolic activities release CO 2 into the blood, which quickly becomes converted to carbonic acid and lowers the pH.
The graph to the right displays so-called "oxygen loading curves" that reveal the effectiveness with which hemoglobin binds oxygen. The more effective the binding, the less oxygen required before hemoglobin becomes fully loaded and the farther to the left a loading curve is shifted. To assess the impact of pH on this process, O 2 loading curves were carried out at three different blood pH values. In the graph, oxygen levels in the blood are presented on the x axis, and for each data point the corresponding % hemoglobin saturation ( %, or percent, is the numerator [top part] of a fraction whose denominator [bottom part] is 100-in this case, a measure of the fraction of the hemoglobin that is bound to oxygen) is presented on the y axis. The oxygen-loading curve was repeated at pH values of 7.6, 7.4, and 7.2, corresponding to the blood pH that might be expected in resting, exercising, and very active muscle tissue, respectively.
Making Inferences At an oxygen level of 40 mm H g , would hemoglobin bind oxygen more tightly at a pH of 7.8 or 7.0?
Explanation
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At an oxygen level of 40 mm Hg, hemoglob...
Essentials of the Living World 5th Edition by George Johnson
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