Myoglobin would be an inappropriate carrier of oxygen to peripheral tissuesbecause:Myoglobin exists in the T, or deoxy state, in muscle tissue.Myoglobin would not release oxygen at the oxygen pressures found in muscletissue.Myoglobin has lower affinity and would lose the oxygen to hemoglobin duringtransport.Myoglobin is only soluble in plasma.Two of the above.

Hemoglobin and Myoglobin are two oxygen binding proteins found in mammals. Myoglobin is an oxygen…

Answered: Myoglobin would be an inappropriate…

Human Physiology: From Cells to Systems (MindTap Course List)

9th Edition

ISBN:9781285866932

Author:Lauralee Sherwood

Publisher:Lauralee Sherwood

Chapter7: The Peripheral Nervous System: Efferent Division

Section: Chapter Questions

Problem 1SQE

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Which of the following statements does NOT apply to the K value in the equation for the oxygen binding curve of myoglobin? It is numerically equal to p50. O A. It is defined as that oxygen partial pressure at which half of the oxygen binding sites are occupied. В. If Y> K, then myoglobin is less than 50% saturated with oxygen. OC. O D. It is a measure of the affinity of myoglobin for oxygen. OE. It is the value of po2 at which Y = 0.5.
Myoglobin’s oxygen-binding curve exhibits a shape best described as— serpentine. hyperbolic. straight. sigmoidal. bell.
As the value of p50 myoglobin for oxygen. increases, decreases decreases, increases decreases, decreases increases, increases None of the above the value of K _--_, resulting in a high affinity of
Match the colour of myoglobin to the ligand bound. brown red pink 1. carbon monoxide 2. nitric oxide 3. water
The shape for curve of oxygen binding to Myoglobin is ___________ and the shape for curve of oxygen binding to Hemoglobin is _________________ Hyperbolic, Hyperbolic Sigmoidal, Sigmoidal Flat, Sigmoidal Hyperbolic, Sigmoidal
Myoglobin and hemoglobin differ in... Question 30 options: the type of prosthetic group used their total oxygen binding capacity the number of sub-units present A and B B and C
Please explain the difference between the oxygen dissociation curve created by myoglobin (asymptotic) versus the oxygen dissociation curve created by hemoglobin (sigmoidal). Why does this occur? Myoglobin O₂ saturation (%) 100 80 60 40 20 0 20 Hemoglobin 40 60 80 100 120 Po₂ (mmHg)
Which of the following statements is correct of BOTH haemoglobin and myoglobin? Acidic conditions increase the affinity for oxygen. The iron atom of the heme prosthetic group is bound to nitrogen atoms at five of six coordination sites. Four oxygen molecules bind to each subunit. Quaternary structure is found in both haemoglobin and myoglobin. Both haemoglobin and myoglobin show the same oxygen binding affinity at different
In 1913, Archibald Hill described an alternative formulation for cooperative processes such as the binding of oxygen by hemoglobin by considering the hypothetical equilibrium Hb+ n0₂ Hb(0₂)n 2 Analysis leads to the Hill equation: n p02₂" ( Y log (₁ x x ) = log Y (^_^) log where Y is the fractional saturation. This equation suggests that a plot of log with slope n. Plots for myoglobin and hemoglobin are shown here: 3 2 1 O -1 -2 -3 P50 + n = nlog (pO,) – n log(P5o) Myoglobin (0.25, -0.25) -1 0 1 2 log (pO₂) (3.0, 2.5) 3 4 (^_^) log 3 2 1 O -1 -2 -3 -4 (0, -3.4) -1 0 Y Y versus log (pO₂) should yield a line Hemoglobin (2.1, 2.5) - (0.7, -2.0) (1.9, 1.3) (0.4, -3.5) 1 2 log (pO₂) - (2.4, 2.4) 3 4
Figure 6 shows the binding of oxygen to myoglobin and haemoglobin (Y-axis: Fraction saturation) when they are exposed to various partial pressures of oxygen (X-axis: pO2). 0.9 0.8 Myoglobin 0.7 0.6 0.5 0.4 Hemoglobin 0.3 0.2 0.1 2 10 12 Po, (kPa) Figure 6 (i) Briefly compare the protein structure of myoglobin to that of haemoglobin. (ii) Based on Figure 6, explain the differences between the functions performed by myoglobin and haemoglobin. Fraction saturation
Which 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.
During maximal aerobic exercise, exercise-induced arterial hypoxemia may result in elite endurance athletes due to which of the following? reduced venous return leads to decreased pulmonary capillary flow rate transit time through the pulmonary capillaries is much shorter oxygen diffusion capacity is no longer calculated using capillary mean PO2 lower venous O2 content increases the PO2 gradient

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