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15 Oct 2018

1.What is the relative intensity (I/Io) of light at 940 nm after traveling through a depth 0.5L of oxygenated hemoglobin?

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Casey Durgan
Casey DurganLv2
16 Oct 2018

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Related questions

These questions are from the Oxygenation of Hemoglobin lab.

1) In this lab experiment, the absorbance was measured at 540 and 556 nm. Pulse oximeters use LED’s that produce red and infrared light at much longer wavelengths. Why is red and infrared light used? What I have so far...--> LED emits red and infrared light that can be abosrbed by Hb and HbO2. A photodetector measures the amount of light that is not absorbed. (Yeah, not sure if this is right or even close)

2) Cyanide can also bind strongly to the heme Fe in hemoglobin. Based on the structure would you expect CN- to bind to hemoglobin more similarly to CO or to O2?

1)How is oxygenated and deoxygenated blood distributed through fourchambers?

2) What is the structure that blood returns to the heartthrough and what chamber of the heart does it lead to?

3) Which chamber pumps oxygenated blood to the entire body,what structure does the blood pass through?

4) What is myocardium and which chamber has the thickest layerof myocardium, why?

5) Where is blood coming from when it enters the leftatrium?

6)What is the purpose of the bicuspid and tricuspidvalves?

7)What is the purpose of the sinoartrial node?

8)What are the papillary muscles?

9) What are purkinje fibers?

10) What would happen if there was a hole in the interatrialseptum or inerventricular septum?

Normal adult hemoglobin is called Hemoglobin A (Hb A). Ninety-eight percent of adult hemoglobin is Hb A and 2% is Hb A2. There are other forms of hemoglobin. For example, the developing fetus has a different kind of hemoglobin than most normal adults. Fetal hemoglobin (Hb F) is synthesized beginning at the third month of gestation and continues up through birth. After the neonate is born, hemoglobin F synthesis declines (because synthesis of the (chain declines) and hemoglobin A is synthesized. By the time the baby is six months old, 98% of its hemoglobin is Hemoglobin A. There is also a mutant form of hemoglobin called Hemoglobin S, which is found in persons with the disease sickle cell anemia. The disease sickle cell anemia is one of the major health problems facing the African-American community. The World Health Organization estimates that 250,000 babies world wide are born with sickle cell anemia. Currently there is no cure. A person afflicted with sickle cell anemia has inherited a defective gene from each parent. The defective gene is the one coding for the β-chain. The amino acid at position 6 on each β chain has been mutated from a glutamate to a valine. Normal α chains have a decreased affinity for the mutated β chains; thus assembly of the HbS tetramer is more difficult. Red blood cells containing HbS form a sickle shape because the Hb S molecules polymerize. Hb S molecules are more likely to polymerize when in the deoxygenated T form than in the oxygenated R form. The polymerized Hb deforms the normal discoid shape of the red blood cells, producing a sickle-shaped cell. The sickle shaped red blood cells become trapped in capillaries and organs, depriving the victim of adequate oxygen supply and causing chronic pain and organ damage.

Glover, R. E., Ivy, E. D., Orringer, E. P., Maeda, H., and Mason, R. (1999) Molecular Pharmacology 55, pp. 1006-1010.

Huang, J., Hadimani, S. B., Rupon, J. W., Ballas, S. K., Kim-Shapiro, D. B., and S. Bruce King (2002) Biochemistry 41, pp. 2466-2474.

S. Bruce King (2003) J.Clin. Invest., 111, pp. 171-172.

1) Why do you think Hb S has higher tendency to polymerize compared to Hb A?

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