You have discovered a new form of mouse myoglobin that has a p50 of 9 Torr. Atapproximately what pO2 would this hemoglobin be 86% saturated with oxygen?85 Torr40 Torr60 Torr55 TorrNot enough information is given to answer this question

The partial pressure of oxygen at which haemoglobin or myoglobin is half saturated with oxygen is…

Answered: You have discovered a new form of mouse…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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5. Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). O UNTREATED 100 a Dсм 23 Torr Symbols: в Dсм 50 Torr x DCM I00 Torr o, 0 Torr DCM; O, 23 Torr DCM A, 50 Torr DCM x, 100 Torr DCM. 80 60 40 (1 Torr = 1 mm Hg.) 20 The solutions were buffered to pH 7.4. 0.5 1.0 1.5 2.0 log p02 (a) (* Hill plots. Label the axes and indicate on both the plot above and the Hill plot where the value of the dissociation equilibrium constant Ka for O2 binding is defined for 0 and 100 Torr of dichloromethane For the curves at 0 and 100 Torr of dichloromethane, draw their equivalent in the form of Kd Hb(O2)n Hb + nO2 % OXYGENATION
Describe the expected differences in the impedance for a fully frozen and fully thawed tissue
Studies of oxygen transport in pregnant mammals show that the O2-saturation curves of fetal and maternal blood are markedly different when measured under the same conditions. Fetal erythrocytes contain astructural variant of hemoglobin, HbF, consisting of two α and two γ subunits (α2 γ2 ), whereas maternal erythrocytes contain HbA (α2β2).(a) Which hemoglobin has a higher affinity for oxygen under physiological conditions, HbA or HbF? Explain.(b) What is the physiological significance of the different O2 affinities?(c) When all the BPG is carefully removed from samples of HbA and HbF, the measured O2 -saturation curves (and consequently the O2 affinities) are displaced to the left. However, HbA now has a greater affinity for oxygen than does HbF. When BPG is reintroduced, the O2 -saturation curves return to normal, as shown in the graph. What is the effect of BPG on the O2 affinity of hemoglobin? How can the above information be used to explain the different O2 affinities of fetal and…
HbA1c is a glycated hemoglobin in which a glucose molecule is covalently bound to the N-terminal valine of a hemoglobin subunit. True False
You've discovered a new organism that contains a mutant form of Hemoglobin (red line on right) and are testing its properties in a lab setting at a neutral pH. You've generated the binding data below comparing it to the wildtype (non-mutant; blue line on left) form. Oxygen binding of a new hemoglobin mutant 1.00 - 0.75- Hemoglobin 0.50 - Wildtype Mutant 0.25- 0.00 - 25 50 75 100 pO2 (torr) 1. How does this mutation seem to impact cooperativity? Hint. Look at the slope of the line. [ Select ] 2. Which variant, the mutant or wildtype, has a higher affinity for oxygen? [ Select ] 3. Which variant is a more effective delivery system to the the muscles (~20 torr)? Select ] Fraction of Hb bounw with Oxygen
I now know the structure difference between myoglobin and hemoglobin , however which exctaly structure difference make myglobin become a oxygen storage ? and not a oxygen transport?? Be specific! details describe how the structure connect to their role. also which exctaly structure difference make hemoglobin become better oxygen transport?? I need the specific structure that contribute to their unique role. I KNOW THE STRUCTURE DIFFERENCE , but don't understand which specific part make myoglobin only bind to oxygen, and not release oxygen
Normal Hgb is referred to as HbA and contains 4 subunits, 2 a-globin chains and 2 B-globin chains, arranged as two dimers of aß. In Sickle Cell Disease, both B-globin chains are altered in the dimers (aßS/aßS). Q3: Which level of structure does the aß/aß and aßS/aßS in HbA and HbS describe?
You are considering transport of Fe3+ out of a biological cell with a membrane potential of -60 mV. What is the value for delta psi in this case? (Make sure you express this value in proper units, i.e., as you would enter this value into the change in free energy of transport equation.)
Why does the dissociation constant change for hemoglobin in high and low 02 concentrations? O Hemoglobin is a tetramer and subunits have decreased dissociation of 02 when a neighboring subunit has bound 02 O Hemoglobin is a monomeric protein with increased dissociation of 02 when a neighboring molecule has bound 02 O Hemoglobin is a tetramer and subunits have increased dissociation of 02 when a neighboring subunit has bound CO O Hemoglobin is a tetramer and subunits have increased dissociation of O2 when a neighboring subunit has bound O2
5. Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). O UNTREATED 100 Symbols: a Dсм 23 Torr • DCM 50 Torr x DCM I00 Torr o, 0 Torr DCM; О, 23 Torr DСМ Д, 50 Torr DСМ x, 100 Torr DCM. 80 60 40 (1 Torr = 1 mm Hg.) 20 The solutions were buffered to pH 7.4. 0.5 1.0 1.5 2.0 log p02 For the curves at 0 and 100 Torr of dichloromethane, draw their equivalent in the form of (a) (* Hill plots. Label the axes and indicate on both the plot above and the Hill plot where the value of the dissociation equilibrium constant Kd for O2 binding is defined for 0 and 100 Torr of dichloromethane Kd Hb(O2)n nO2 Hb + Be sure to label the axes, indicate the units on both axes, and make the Hill plot so that the values of Kd are equivalent to those on the saturation plot above. Indicate whether cooperativity, as indicated by the Hill…
Below is a list of hypothetical Hemoglobin variants. Circle the name of the variant that is most likely to show an increase in BPG binding. Does such a hypothetical variant cause an increase or decrease in hemoglobin's affinity for oxygen? A. Hb Miami: Leu is substituted with Pro in an alpha helix B. Hb California: Val is substituted with Lys at pH 7.0 C. Hb New york: Tyr is substituted with Met, which disrupts the hydrogen bonding at the a131 interface. D All of the above
Identify the incorrect statement regarding the polypeptide, Myoglobin. Select one: a. The interaction between Myoglobin and O2 is homotopic in nature as indicated by a Hill coefficient n = : 1 b. Myoglobin is found predominantly in muscle tissue because it facilitates oxygen diffusion. c. The majority of Myoglobin's secondary structure is composed of alpha-helices d. Myoglobin has a higher affinity for oxygen than Hemoglobin e. Myoglobin serves as an oxygen storage protein as suggested by its hyperbolic binding of 02

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You have discovered a new form of mouse myoglobin that has a p50 of 9 Torr. At approximately what pO2 would this hemoglobin be 86% saturated with oxygen? 85 Torr 40 Torr 60 Torr 55 Torr Not enough information is given to answer this question