
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Question

Transcribed Image Text:Which of the following is incorrect about 2,3-bisphosphoglycerate (BPG)?
It is highly (-) charged
b. It prevents binding of O₂ to hemoglobin
Oc. It binds only to the relaxed (oxy) conformation of hemoglobin
Od. It binds in the space between the four subunits of hemoglobin
a.
Expert Solution

This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
Step by stepSolved in 2 steps

Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Fetal hemoglobin binds 2,3 BPG with greater affinity than adult hemoglobin.TrueFalsearrow_forwardBelow is the O₂ binding curve for adult Hb in whole blood (containing BPG) shown in red (labelled Hb). Fraction of Hb bound with Oxygen 1.0 0.8 0.6 0.4 0.2 0.0 0 20 40 pO2 (torr) 60 80 ABC c. Which curve lacks cooperativity? [Select] Hb 100 a. Which curve is the best representation for stripped Hb (pure hemoglobin with heme, but no other small allosteric molecules associated)? [Select] b. Which curve has the lowest affinity (as measured by the p50)? [Select]arrow_forwardIn Charles’ blood, the partial pressure of CO in the blood (0.4 mm Hg) is far lower than the partial pressure of O2, yet the percent saturation of hemoglobin by each gas is approximately equal. What does this tell you about the affinity of hemoglobin for CO?arrow_forward
- Suppose a hypothetical "molecule X" binds to hemoglobin (at a different site than the O2 binding site) and stabilizes the T state. How would you identify this effector? a. Positive homotropic effector b. Negative homotropic effector c. Positive heterotropic effector d. Negative heterotropic effectorarrow_forwardWhy is the decreased affinity of fetal hemoglobin for BPG advantageous? With fewer BPG molecules bound to heme, there are more heme residues available for O2 binding. O A. B. Decreased BPG binding biases the fetal hemoglobin toward the R state. C. More free BPG is available to bind to adult hemoglobin, resulting in a shift to the R state. BPG is more available to bind to fetal myoglobin. helping to release O2 in fetal muscle tissue. D. 47arrow_forwardWhich of the following statements is true for Bohr effect: a. Bohr effect describes carbon monoxide poisoning. b. Bohr effect prevents oxygen binding to hemoglobin. c. Bohr effect allows effective oxygen discharge in tissues due to higher acidity (decreased pH) than in lungs. d. Bohr effect allows effective oxygen discharge in tissues due to lower acidity (increased pH) than in lungs.arrow_forward
- There is an animal that uses almost 100 percent of the oxygen in its blood. Analyzing the Hb of this animal, it’s found that 2,3-BPG does not bind to Hb, but bicarbonate ions do. Knowing that bicarbonate ions are strong negative allosteric effectors, what do you make of these findings? Why is the animal’s Hb not responsive to 2,3 BGP, but responsive to bicarbonate ions?arrow_forwardIn the absence of 2,3-bisphosphoglycerate, the binding of oxygen by hemoglobin: a. is characterized by cooperativity b. resembles that of myoglobin c. binds at the end of the hemoglobin molecule d. is stabilized as the deoxy conformation of hemoglobin for the release into capillariesarrow_forwardCarbon monoxide (CO) is a colorless, odorless gas produced during combustion of fuels (for example, by car engines and furnaces). The following graph depicts an oxygen dissociation curve in the absence and presence of varying amounts of carbon monoxide. Based on these results, in the presence of 20% CO, when PO2 is 90mmHg you should expect each hemoglobin molecule to have _____ molecule(s) of O2 bound a) 1 b) 2 c) 3 d) 4arrow_forward
arrow_back_ios
arrow_forward_ios
Recommended textbooks for you
- Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSONBiology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStaxAnatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
- Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & CompanyLaboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education

Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON

Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax

Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,

Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:9780815344322
Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:W. W. Norton & Company

Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.

Inquiry Into Life (16th Edition)
Biology
ISBN:9781260231700
Author:Sylvia S. Mader, Michael Windelspecht
Publisher:McGraw Hill Education