how does the rate of glycolysis in red blood cells affect oxygen binding to hemoglobin?
Human erythrocytes (red blood cells) have no mitochondria. Since the mitochondria are the cellular site for oxidative metabolism of fatty acids, erythrocytes cannot oxidise fatty acids to release energy. The erythrocytes also cannot fully oxidise glucose (to carbon dioxide and water) because this is also a mitochondrial process, so they have to rely upon anaerobic glycolysis. The end product of anaerobic glycolysis is pyruvate, and erythrocytes reduce this to lactate (to recycle the NADH that is produced during glycolysis) and then export this lactate into the blood for further metabolism by the liver.
2,3-BPG is present in human red blood cells. It binds with great affinity with deoxygenated hemoglobin.That's the reason the curve for hemoglobin in red blood cells is different with respect to the pure hemoglobin curve.
2,3-BPG is an allosteric effector to hemoglobin.2,3-BPG is a naturally occurring molecule that is produced as an intermediate in the glycolysis process. Deoxyhemoglobin in the T-state is a very unstable molecule and this drives the equilibrium towards the R-state, which means that deoxyhemoglobin will not exist for long and the majority of the hemoglobin will be bound to oxygen (i.e have a high affinity for oxygen). However in the presence of 2,3-BPG, this molecule will bind to the center pocket found in hemoglobin, thereby stabilizing the T-state of hemoglobin and allowing it to exist without quickly converting into the relaxed state. That is, by binding to hemoglobin, 2,3-BPG decreases hemoglobins affinity for oxygen, thereby shifting the entire oxygen-binding curve to the right side. This is what allows the hemoglobin to act as an effective oxygen carrier in the body, unloading about 66% of oxygen to exercising tissue.
The major role of red cells in binding, trans-
porting, and releasing oxygen and carbon dioxide
is a passive activity that uses, not consumes, these
gases. The erythrocyte's limited metabolic
processes, which include the Embden-Meyerhof
pathway and the hexose monophosphate shunt,
provide energy to accomplish several of the cell's
functions.
how does the rate of glycolysis in red blood cells affect oxygen binding to hemoglobin?
Hemoglobin is the compound in red blood cells that carries oxygen to the body. The distribution of hemoglobin in women in g/dl of blood is approximately bell shaped with mean 14 and standard deviation 1. According to MedicineNet.com, healthy hemoglobin levels range from 12 to 16. Based on the Empirical Rule, what percent of women have healthy hemoglobin levels?
Hemoglobin is the oxygen transport protein in the red blood cells of all vertebrates. It's emperical formula is C738H1166N203O208S2Fe. It's molecular mass is 65332.91 amu, what is the molecular formula of hemoglobin? How do I solve this problem?
_7. Hemoglobin is a protein in red blood cells that is responsible for transporting oxygen throughout the body. Hemoglobin is made of four separate protein (polypeptide) chains that come together to form a functional protein, What is the highest level of protein structure in hemoglobin? A) Primary B) Secondary C) Tertiary D) Quaternary
Hemoglobin is the oxygen-transport protein in red blood cells and contains 0.340% iron (Fe) by mass. If a blood sample is found to have 12.0 g/dL of hemoglobin, how many iron atoms are in a human body that has 5.0 pints of this blood? Note that d stands for the prefix deci- meaning 1/10, 1 pt = 473.176 mL, and NA = 6:022 X 10^23.
The following results represent the oxygen binding activity of purified myoglobin, purified hemoglobin, and hemoglobin in human blood cells. pO2 (Torr) Fraction of purified myoglobin with O2 pO2 (Torr) Fraction of purified hemoglobin with O2 pO2 (Torr) Fraction of hemoglobin in red blood cells with O2 0.5 0.161 0.1 .00315 10.6 0.10 1.0 0.277 0.35 .0099 19.5 0.30 2.0 0.434 0.794 .0306 27.4 0.50 3.0 0.535 1.748 .0909 37.5 0.70 4.0 0.605 2.884 .24 50.4 0.85 6.0 0.697 4.467 .50...
104 Homework 6 4. (15 points): Hemoglobin (Hb) is the main oxygen transport protein in the blood. Each hemoglobin molecule can transport four oxygen atoms at a time, one at each of its four iron-based binding sites. The binding of O2 to hemoglobin is a pH-dependent equilibrium, simplified as: Use Le Chatelier's Principle to answer the following questions: a) What form of hemoglobin, HbH" or Hb(Ojle, would be favored in the lungs? What form would be favored in the cells...
how do the sickled red blood cells vary from normal red blood cells?How might this affect their ability to serve within the circulatory system?
1. How can hemoglobin deliver oxygen to myoglobin in muscle tissue cells? (use oxygen binding curve, T-state and R-state, sigmoidal, cooperativity, Bohr effect, carbon dioxide, and 2,3-BPG)
5. Hemoglobin is the protein found in red blood cells that transports oxygen from your lungs to your cells. Below is a segment of the DNA sequence that codes for a normal hemoglobin protein (the entire gene is much longer). Using the DNA sequence provided, transcribe the sequence into mRNA. Use the bottom strand as the coding strand. 5' ACTGCCCATGGTGCAC CIGACTCCTGAGGAG 3' 3' TGAC GG GIACCA CGT GGA CIGAG GACTCCTC 5 6. For hemoglobin, translate the mRNA strand from step...
As the red blood cells travel throughout the body they "lose" oxygen and become only partially saturated with oxygen. Where does the equilibrium lie now? Explain using Le Chatelier's Principle. If the blood travels through an area that has a very low concentration of oxygen, such as actively contracting muscle cells, the hemoglobin will become nearly empty of oxygen. Again, can you explain what is happening using Le Chatelier's Principle?