BIOLOGY:CONCEPTS+APPL.(LOOSELEAF)
10th Edition
ISBN: 9781305967359
Author: STARR
Publisher: CENGAGE L
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Textbook Question
Chapter 35, Problem 4CT
A developing fetus gets oxygen from its mother’s blood. Fetal capillaries run through pools of maternal blood in an organ called the placenta. As fetal blood runs through these capillaries, it exchanges substances with the maternal blood around the capillary. The hemoglobin made by a fetus is different than that made after birth. Fetal hemoglobin binds oxygen more strongly at low oxygen levels than normal hemoglobin. How would fetal hemoglobin’s somewhat higher affinity for oxygen benefit the fetus?
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During pregnancy a special fetal hemoglobin was made with the following characteristics:
It binds oxygen with an affinity lower than adult hemoglobin.
It does not bind carbon monoxide.
It is a monomer.
It does not use heme as a co-factor.
It binds oxygen with an affinity higher than adult hemoglobin.
In carbon monoxide (CO) poisoning, CO binds to the heme of hemoglobin much tighter than oxygen (O2). What effect will this have on the ability of the tissues to get oxygen?
Group of answer choices
There will be no effect.
CO will deliver oxygen to the tissues.
Hemoglobin will bind more O2 and deliver more oxygen to the tissues.
More hemoglobin will be produced to deliver oxygen to the tissues.
Hemoglobin will bind less O2 and deliver less oxygen to the tissues.
After your exercise routine at the gym, you sit with friends drinking a glass of water to cool off. Select a single word from list
and place into each blank to make it correct. Not all terms will be used.
40 mmHg
right
increases
As you cool off, metabolism at the skeletal muscles decreases, and the
oxygen saturation curve shifts
affinity for oxygen
because hemoglobin's
. Under these conditions, hemoglobin
20%
is
likely to release oxygen.
decreases
At the same time, the partial pressure of oxygen at the systemic
capillaries changes from about
to
less
Carbon dioxide released from the skeletal muscle cells during vigorous
exercise can make the blood slightly more acidic. This results in
hemoglobin having a
affinity.
left
oxygen saturation or oxygen
higher
40%
20 mmHg
lower
more
Chapter 35 Solutions
BIOLOGY:CONCEPTS+APPL.(LOOSELEAF)
Ch. 35 - Respiratory proteins such as hemoglobin...Ch. 35 - In______, gas exchange occurs at the body surface...Ch. 35 - Countercurrent flow of water and blood increases...Ch. 35 - In human lungs, gas exchange occurs at the...Ch. 35 - Prob. 5SACh. 35 - During inhalation, ________. a. the thoracic...Ch. 35 - What type of metal associates with hemoglobin?Ch. 35 - Prob. 8SACh. 35 - Prob. 9SACh. 35 - The medulla oblongata ___________. a. produces...
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- After oxygen diffuses into lung capillaries, it also diffuses into _______ and binds with _______. a. tissue fluid; red blood cells b. tissue fluid; carbon dioxide c. red blood cells; hemoglobin d. red blood cells; carbon dioxidearrow_forwardWhich of the following are most closely associated with oxygen transport? (a) red blood cells (b) platelets (c) neutrophils (d) basophils (e) lymphocytesarrow_forwardWhich of the following statements about oxygen transport is TRUE. Increases in temperature and decreases in pH cause myoglobin to release oxygen to improve delivery to the hemoglobin in muscles. A molecule of myoglobin has higher oxygen binding capacity than a molecule of hemoglobin. Myoglobin has a higher oxygen affinity than does hemoglobin. Fetal hemoglobin has a lower affinity for oxygen than maternal hemoglobin, which makes it better suited to extract oxygen from the maternal circulation.arrow_forward
- With the appearance of strong oxidizers in blood in erythrocytes one of the following substances is formed first of all: 1. carbhemoglobin 2. carboxyhemoglobin 3. oxyhemoglobin 4. methemoglobin 5. deoxyhemoglobinarrow_forwardPlace a single word into each sentence to make it correct saturation The relationship between hemoglobin and Po2 is shown by an oxyhemoglobin dissociation curve. rises lowers At low Po2, the curve slowly load When the curve rises there is a rapid increase in oxygen loading. deficiency When the first heme group binds a molecule of oxygen, changes conformation to accept a second carbon dioxide Oxygen. Eventually at high Po2 levels, the hemoglobin approaches 100 % saturation and can not hemoglobin more oxygen.arrow_forwardAnswer the following questions about hemoglobin. The number of high affinity binding sites in the R form of hemoglobin is .The number of low affinity binding sites in the R form of hemoglobin is .The number of O2 molecules that need to bind to convert hemoglobin from the T to R form is .The number of high affinity binding sites in the T form of hemoglobin is .The number of low affinity binding sites in the T form of hemoglobin isarrow_forwardThe part of hemoglobin that binds iron is O alpha globulin 2 Obeta globulin 2 alpha globulin 1 O beta globulin 1 hemearrow_forwardFetal hemoglobin binds 2,3 BPG with greater affinity than adult hemoglobin.TrueFalsearrow_forwardWhen a person develops a fever, which of the following statements hemoglobin saturation are correct? - Modify the structure of hemoglobin and decrease its affernity for O2 - Can shift the O2-hemoglobin dissociation curve to the right - Decrease O2 unloading occurs in the tissue - Modify the structure of hemoglobin and increase its affernity for O2 - Can shift the O2 hemoglobin dissociation curve to the left - Enhance O2 unloading occurs in the tissuearrow_forwardThe function of hemoglobin is to carry dissolved blood gases. carry bicarbonate ion. aid in the process of blood clotting. produce antibodies. stimulate erythropoiesis.arrow_forwardWhich of the following is FALSE about hemoglobin? O Hemoglobin only binds oxygen Every subunit of hemoglobin contains a heme group with an iron atom Hemoglobin contains four subunits As 02 molecules bind to hemoglobin, hemoglobin affinity for 02 increases All of the above are truearrow_forwardSelect all statements that correctly describe hemoglobin and myoglobin structure. Each hemoglobin molecule can bind four oxygen molecules; each myoglobin can bind one oxygen molecule. Molecular oxygen binds irreversibly to the Fe(II) atom in heme. Each iron atom can form six coordination bonds. One of these bonds is formed between iron and oxygen. Hemoglobin and myoglobin are heterotetramers. The heme prosthetic group is entirely buried within myoglobin. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron (Fe) atom. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron.arrow_forwardarrow_back_iosSEE MORE QUESTIONSarrow_forward_ios
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