INTRO FOR 329 LAB- HEMOGLOBIN - Abstract Experiments were...

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Abstract: Experiments were run to observe the effects that oxygen had on hemoglobin (from horse erythrocytes) molecules. These experiments included running spectrophotometer absorption readings for oxygenated and deoxygenated samples, followed by running the same procedures through different types of buffers while trying to reoxygenate the hemoglobin after deoxygenating it. The erythrocytes was put through absorption measurements along with neutral buffers to see what affects oxygen had on the conformational change of hemoglobin molecules and how the heme groups and globins would react to newly bonding oxygen molecules. The hemoglobin was then deoxygenated and stripped off of its allosteric enzyme and a negative correlation was observed. The more you remove or damage the oxygen from the hemoglobin by nitrogen, the worse the absorptions and the worse the hemoglobin activity. The same procedure was done but this time it was reoxygenated after being deoxygenated. A positive correlation showed that even after you removed the molecules successfully of oxygen, you can go back and add the oxygen back and the activity of the enzyme will continue to rise back up. This shows that removal of oxygen doesn’t destroy or alter the configuration of hemoglobin and that the effects are reversible. The same procedures were repeated but at a different pH. This was to observe the effect of hydrogen ions on oxygenated hemoglobin molecules and to witness the ‘Bohr’ effect. It was observed that oxygen is a homotropic effector that has a positive effect on horse hemoglobin and acts like an allosteric effector. It is also observed that hydrogen ions are proved to be negative heterotropic effectors that cause a decrease in function of hemoglobin due to the Bohr’s effect. Introduction: Our red blood cells contain hemoglobin. Hemoglobin is a tetrameric protein, in the blood, that contains iron. Hemoglobin is developed in the bone marrow. It is formed in cells in the bone marrow. In addition, red blood cells serve as an oxygen transport system. This is done by the iron in the hemoglobin. The iron binds to the oxygen, therefore, helping the oxygen to travel around the body. Hemoglobin is made out of four
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heme groups. Heme is ring-like (porphyrin) structure that has one iron bind to it. Subsequently, hemoglobin has four polypeptide chains that contain four iron groups which help bind four oxygen atoms. They almost entirely consist of α-helices. As for ‘globin’, it contains two linked pairs of polypeptide chains. Globins have 8 helices in a characteristic fold. Binding becomes easier with the heme group between the two dimmers. Recently this year, it was found that a protein called HRI regulates the iron that is retained in the blood. Without this HRI protein, “the iron is retained but never puts it to work” – Science Daily, Oct 12, Jane-Jane Chen, Sijin Liu. However, myoglobin, the oxygen storage of muscle,
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INTRO FOR 329 LAB- HEMOGLOBIN - Abstract Experiments were...

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