Haemoglobin

Jim’s body has slowed down and was giving 80% body effort while ignoring the pain. #2. What changes in Jim's muscles promote unloading of O2 from hemoglobin for use by the muscles cells? When Jim's muscles and cells are feeling the burning sensation this is caused by the O2 from hemoglobin when these cells are being used excessively. He used up his hemoglobin by vigorously rowing the boat up to its maximum speed.

As the concentration of hemoglobin in the Red Blood Cells falls below normal, the total Red Blood Cell count consequently decreases. Therefore, oxygen cannot be adequately carried. (http://www.mayohealth.org/mayo/pted/htm/iron.htm).

“Erythrocytes contain haemoglobin, an important respiratory pigment that is essential for human life” (Strech, Beryl; Whitehouse, Mary;, 2010) Haemoglobin is very important because it is an iron-containing protein.

 Once the oxygen-depleted cells are in the lungs, they travel into the alveoli where they lose their CO2 and trade it for oxygen. The oxygen is able to stay with the red blood cells because the cell have hemoglobin which is a protein which binds with oxygen.

3) Explain why O2 requires the transport protein Hb and state the percentage of oxygen transported around the body by Hb. Only 1.5 percent of oxygen in the blood is dissolved directly into the blood itself. Majority of oxygen which is 98.5 percent joins to hemoglobin and is then carried to the tissues. 4) Explain where in the body the forward reaction and reverse reactions are most likely to occur, referring to partial pressures of O2 in your explanation.

The blood protein in Methemoglobinemia are unable to carry oxygen, which makes it harder for the tissue to get the amount of oxygen

Methemoglobinemia is a hemoglobinopathy where the concentration of methemoglobin in the blood is more than 1% of the total hemoglobin [3]. Normal hemoglobin has a reduced ferrous iron (Fe 2+) while methemoglobin has an oxidized ferric iron (Fe 3+). The change in valence prevents methemoglobin from being able to carry oxygen [4, 9]. There are mechanisms in place to reduce the amount of methemoglobin in the blood [2]. Cytochrome b5-Methemoglobin reductase and nicotinamide adenine dinucleotide phosphate (NADPH) methemoglobin reductase enzymes are responsible for reducing the amount of methemoglobin in the blood [9].

Platelets and leukocytes are less than 0.1% of formed elements but nearly 99.9% are nuclei-lacking red blood cells, whose biconcave disk-shape increases surface area and allows for the diffusion of oxygen (Martini et al., 2015). Erythrocytes contain hemoglobin proteins, where each protein has four iron-containing heme groups that can bind one oxygen molecule each (Surgenor, 2013). In other words, each hemoglobin protein can carry four oxygen molecules and there are over 250 million hemoglobin proteins per cell.

Haemoglobins are formed when four Globin molecules link together.

The red blood cells have an unusual structure compared to other cells in the human body, as it lacks a nucleus, mitochondria or endoplasmic reticulum (###). However, the enzyme component in the red blood cells allow it to produce small amount of energy (ATP from glucose). The mature red cell contains about 34 percent haemoglobin (a complex iron bearing pigment that transports oxygen). It gives a red colour to the cell, with a combination of heme and globin (###). Haemoglobin is the functional component of the cell, contained in the interior of the cell, and the outer surface of the cell is surrounded by a cell membrane. It has a pale, greenish yellowish appearance when unstained, and reversibly combined with oxygen and, to a lesser extent with carbon dioxide (###). The average concentration of haemoglobin is 14 g/100 ml blood in women and 16 g/100 ml in men (###). The production of the erythrocytes, occur primarily in the red marrow of the spongy bones. The vast surface area is important in the transport of oxygen from the lungs to the tissue because of quick exchange of oxygen in both sites that occurs across the red cell surface (@@@). An adult female has approximately 4.8 million/cu mm red cells, and adult male has approximately 5.5 million/cu mm red cells. An erythrocyte can stay between 80 to 120 days in

Myoglobin is a substance which helps muscle use oxygen. When the muscle is damaged, the myoglobin is released into the bloodstream. It is filtered out of the bloodstream

The other type of artificial blood is more of a blood substitute as it is derived from either outdated bovine or human red blood cells. It is known as Hemoglobin Based Oxygen Carriers (HBOC), Hemoglobin which is the oxygen carrying protein molecule found in red blood cells is extracted from the obsolete red blood cells through ultrafiltration and purification. The Hemoglobin must undergo specific processes in an attempt to prevent the Hemoglobin from disassociating from its natural four-chain configuration (Fridey 3). There is numerous methods of chemically altering the Hemoglobin to increase the molecules size so it does not dissociate and break down. The two main processes of enlarging the

Hemoglobin is present in red blood cells of the body and transport oxygen from lungs to the rest of the human body (National, 2015). Humans carry different types of hemoglobin, but there are three common types found in the gel electrophoresis. One of the test blood that help people to diagnose any disease is the hemoglobin electrophoresis. Hemoglobin electrophoresis test looks at the different types of hemoglobin in the blood, and can help diagnose the type of anemia that the person could have (National, 2014). The three common types of hemoglobin presents in humans are normal hemoglobin, sickle trait hemoglobin, and sickle cell hemoglobin. Abnormal hemoglobin, called hemoglobin S, causes sickle cell disease (SCD). The sickle cell hemoglobin

Haemoglobin is a protein molecule found in red blood cells (RBC). Its role in the body is to transport oxygen from the lungs to the body 's tissues and then returns carbon dioxide from the tissues back to the lungs. The transportation of oxygen is only possible when haemoglobin (Hb) within the RBC binds to oxygen. (Martini & Nath, 2006)

Oxygen is not very soluble in an aqueous solution such as blood so it needs to bind to hemoglobin in order to be transported. Each of hemoglobin iron ions can bind to one oxygen molecule which means that hemoglobin can carry four oxygen molecules at a time. The reason why oxygen binding to hemoglobin is very efficient is because of a process called “cooperative” binding.