EBK BIOLOGY
5th Edition
ISBN: 8220100667978
Author: Maier
Publisher: PEARSON
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Chapter 19, Problem 4LTB
Summary Introduction
Introduction:
The heart is the muscular organ which is approximately the size of one’s fist. It is located behind and slightly left of the breastbone. The function of the heart is to pump the blood by arteries and veins. The whole network of arteries, veins, and heart is termed as cardiovascular system.
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Carbon monoxide (CO) is a colourless, odourless gas that result from the burning of
hydrocarbons, such as in a poorly functioning furnace or vehicle emissions. CO can bind
with hemoglobin to form carboxyhemoglobin. Hemoglobin's affinity for CO is 200 times
greater than its affinity for oxygen. The initial symptoms of carbon monoxide poisoning
are flu-like, such as dizziness, headache and vomiting. However, when left unchecked,
CO poisoning can result in unconsciousness, loss of blood flow to the vital organs and,
eventually, death.
(Source: Bleecker, M.L. (2015). Carbon Monoxide Intoxication. Handbook of Clinical Neurology. Elsevier B.V.)
5.
Name the gases normally carried by hemoglobin in the body. Using your knowledge
of the circulatory and respiratory systems, provide a possible explanation for the
symptoms of carbon monoxide poisoning.
The part of hemoglobin that binds iron is
O alpha globulin 2
Obeta globulin 2
alpha globulin 1
O beta globulin 1
heme
biliverdin
macrophages
urobilinogen
bilirubin
Erythrocytes are continually replaced. Worn-out erythrocytes are lysed in the spleen as they pass through splenic
cords in the spleen.
digest these cell parts, and separate heme from the globin units
of hemoglobin. The globin proteins are broken down into amino acids and recycled. The heme pigment is
converted into
, then
, and released into the blood. It is
concentrated in urine, producing its yellow color. The liver removes additional bilirubin and secretes it into bile.
When released into the small intestine, bacteria transform it into
which makes feces
brown.
Chapter 19 Solutions
EBK BIOLOGY
Ch. 19 - Describe how contraction of the diaphragm allows...Ch. 19 - Describe the movement of blood through the four...Ch. 19 - Alveoli are ___________. small air sacs at the...Ch. 19 - Prob. 4LTBCh. 19 - Prob. 5LTBCh. 19 - Prob. 6LTBCh. 19 - Prob. 7LTBCh. 19 - Prob. 8LTBCh. 19 - Heart attacks ___________. are typically caused by...Ch. 19 - Prob. 10LTB
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- What units describe Hemoglobin and in your own words describe what Hemoglobin is What units describe Hematocrit and in your own words describe what Hematocrit is Pick one condition that casues high or low hemoglobin and explain why it causes high or low condition Pick one condition that casues high or low hematocrit and explain why it causes high or low conditionarrow_forwardHemoglobin will bind oxygen and release CO2 in places where there is a higher concentration of O2, lower concentration of CO2, lower temperature and lower acidity (as it is in lungs) and will do the reverse – release oxygen and bind CO2 - in places where there is a lower concentration of O2, higher concentration of CO2, higher temperature and higher acidity (as it is in working muscles). True False While white blood cells never leave the circulation, red blood cells regularly leave it and travel by lymphatic system or find home in other tissues, e.g., lymph nodes, spleen, etc. True False Blood clotting (coagulation) is a complex process involving many factors and it exhibits positive feedback loops: many of the factors also stimulate production of their own precursors. B lymphocytes mature in the thymus while T lymphocytes mature in the bone marrow True False Antibodies are molecules on the surfaces of foreign…arrow_forwardHemoglobin is a ____________ with ____________ structure, and its main role is to carry ____________. carbohydrate, tertiary level, red blood cells (erythrocytes) protein, symmetrical, platelets protein, quaternary level, oxygen/carbon dioxide lipid, cis-saturated, phospholipids to and from the cell membranearrow_forward
- Which substance is transported by hemoglobin? urea water охygen O nitrogenarrow_forwardWhich five statements about hemoglobin and myoglobin structure are true? Each iron atom can form six coordination bonds. Two of these bonds are formed between iron and oxygen. Molecular oxygen binds reversibly to Fe²+ in heme. Heme is composed of an organic protoporphyrin component and a metal atom. By itself, heme is not a good oxygen carrier. It must be part of a larger protein to prevent oxidation of the iron atom. Each hemoglobin or myoglobin molecule can bind four oxygen molecules. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron atom.arrow_forwardWhich of the following statements regarding the transport of oxygen by hemoglobin is correct? Upon binding of oxygen to heme, a shift in the position of the distal His ultimately induces the switch from T to R states When fully bound to oxygen, AG(R-state)arrow_forwardHemoglobin can exist in one of two forms. What are they?arrow_forwardDescribe the function of each of the following in hemoglobin. Fe; Distal His; Proximal His; Alpha/beta interface; Protoporphyrin IX;arrow_forwardCarbon monoxide binds to hemoglobin more readily than oxygen. Why is this dangerous?arrow_forwardThe following statement describes which level of structure of the hemoglobin molecule? "Each chain is stabilized by electrostatic interactions between -COO- and -NH3+ of amino acid side chains." Primary Second Tert Quatarrow_forwardReduction in pH of blood will -------------------------- (descrease/increase) the affinity of hemoglobin with oxygen.arrow_forwardThe hemoglobin molecule Is made inside of the liver Carries around 15 percent of the oxygen in the blood Turns dull brownish red when oxygen is bound to it. Consists of 2 globin chains and 2 iron groups Is contained inside of red blood cells.arrow_forwardarrow_back_iosSEE MORE QUESTIONSarrow_forward_ios
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