what is function of haemoglobin and what is the physical phenomenon behind it? how it works in our body?

Answer 1

Hemoglobin is an iron-protein compound in red blood cells that gives blood its red color and transports oxygen, carbon dioxide, and nitric oxide. Hemoglobin is present in all but the least complex of animals. It carries oxygen from the lungs or gills, where blood is oxygenated, to body cells. When saturated with oxygen, hemoglobin is called oxyhemoglobin. After releasing oxygen to the body tissues, hemoglobin reverses its function and picks up carbon dioxide, the waste product of cellular respiration, for transport to the lungs, where it is expired. When saturated with carbon dioxide, hemoglobin is known as carboxyhemoglobin.

In 1996 scientists discovered that, in addition to oxygen and carbon dioxide, hemoglobin takes up and releases a third gas, nitric oxide. Nitric oxide plays an important role in regulating blood pressure by relaxing the blood vessel walls, thus increasing blood flow. Hemoglobin controls the expansion and contraction of blood vessels, and thus blood pressure, by regulating the amount of nitric oxide to which the vessels are exposed.

Hemoglobin is contained entirely in the red blood cells, amounting to perhaps 35 percent of their weight. To combine properly with oxygen, red blood cells must contain adequate hemoglobin. Hemoglobin, in turn, is dependent on iron for its formation. A deficiency of hemoglobin caused by a lack of iron in the body leads to anemia.

Hemoglobin carries more than 20 times its volume of oxygen. Some chemicals, such as carbon monoxide, combine so firmly with hemoglobin that it can no longer combine with oxygen and asphyxiation results.

After a life of perhaps 120 days, red blood cells are destroyed in the spleen, or in the course of circulation, their hemoglobin is broken into its constituents, including iron, which enters new blood cells formed in the bone marrow.

When blood vessels rupture, as in an injury, the red cells are released and escape into tissue, where they are broken down. The hemoglobin is converted into bile pigments, the color of which is responsible for the appearance of bruises.

Alterations in the structure of hemoglobin can lead to life-threatening illnesses. The most important of these conditions is sickle-cell anemia, which involves a hereditary change in one of the amino acids that make up hemoglobin. The thalassemias are a group of hereditary diseases of similar origin.

KKG

Answer 2

Function Of Haemoglobin

Answer 3

Haemoglobin transports oxygen vital to the respiration and survival of cells that make up the body. Its not a physical but a chemical phenomenon. The Oxygen atom bonds to the iron atom in haemoglobin. This oxygen is then intercahanged with CO2 at the cell surface.

Every haemoglobin molecule has four iron atoms and thus can carry 4 oxygen atoms at one go.

Answer 4

Hemoglobin or haemoglobin (frequently abbreviated as Hb) is the iron-containing oxygen-transport metalloprotein in the red cells of the blood in mammals and other animals. Hemoglobin in vertebrates transports oxygen from the lungs to the rest of the body, such as to the muscles, where it releases the oxygen load. Hemoglobin also has a variety of other gas-transport and effect-modulation duties, which vary from species to species, and which in invertebrates may be quite diverse.

The name hemoglobin is the concatenation of heme and globin, reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme (or haem) group; each heme group contains an iron atom, and this is responsible for the binding of oxygen. The most common types of hemoglobin contains four such subunits, each with one heme group.

Mutations in the genes for the hemoglobin protein in humans result in a group of hereditary diseases termed the hemoglobinopathies, the most common members of which are sickle-cell disease and thalassemia. Historically in human medicine, hemaglobinopathies were the first diseases to be understood in mechanism of dysfunction, down to the molecular level.

Hemoglobin is synthesized in the mitochondria of the immature red blood cell throughout its early development from the proerythroblast to the reticulocyte in the bone marrow, when the nucleus has been lost. Even after the loss of the nucleus, residual ribosomal RNA allow further synthesis of Hb until the reticulocyte loses its RNA on entering the vasculature. Hemoglobin is chemically represented by (C2952H4664N812O832S8Fe4).

Answer 5

The haemoglobin molecule is made up of four polypeptide chains (a tetrameric haemprotein) (Alpha 1, Beta 1 , Alpha 2, Beta 2), non-covalently bound to each other. There are four haem-iron complexes. They are found in erythrocytes where it is responsible for binding oxygen in the lung. They are also responsible for transporting the bound oxygen throughout the body for aerobic metabolism.

Click here for a spacefill view of the haemproteins and all the water molecules on the protein surface.


Each chain holds a haem group containing one Fe++ atom.

Blue atoms represent NITROGEN

Grey atoms represent CARBON

Red atoms represent OXYGEN

Orange atoms represent IRON (Fe)

Spacefill view of atoms that make up haem units.

An elemental oxygen molecule binds to the ferrous iron atom in the lungs where oxygen is abundant, and is released later in tissues which need oxygen.

Answer 6

haemoglobin is the carrier of oxygen in our body. haemoglobin consists of an iron compound which helps oxygen bind to it. when the haemoglobin reaches the parts of the body which need oxygen the oxygen in the haemoglobin is exchanged with the cell in return for carbondioxide, this transfer takes place due to change in ph of the cell with less oxygen due to which oxygen at that ph binds more easily with the cell than the haemoglobin molecule

Answer 7

I like what you are attempting to say here but I can't go along with the analogy. The Holy Spirit enters our bodies not the soul of believers. And He doesn't course through us as blood through our veins. I see it more like the Holy Spirit taking up residency within a house (or temple which we are) and setting up housekeeping. The more we allow Him to do His job the better we are for it. The cleaner He makes us the better we represent the Landlord which will make us more desireable to others. Sometimes analogies help and sometimes they hinder. A lot of people when witnessing will ask another, "Would you like to invite Jesus into your heart." This will even make young children ask ... Will He fit? and adults ... Is this person whacked out? In some cases I've seen children frightened by the prospect of Jesus trying to get in their heart. I think we need to really consider the connotation of how any anaolgy we use will affect the hearer.

Answer 8

Hemoglobin Function

Answer 9

Hemaglobin is very inportant, because it allows the Oxygen molecule to bond with the blood cell to transport O2 throughout the body. It also acts as a lubricant, to easily move throughout the bodies circulatory system..

Answer 10

Haemoglobin, most prevalent of the special blood pigments that transport oxygen; it is present in all but the least complex of animals. Haemoglobin carries oxygen from the lungs or gills, where blood is oxygenated, to body cells. When saturated with oxygen it is called oxyhaemoglobin and is a bright red colour. After haemoglobin releases oxygen to the body tissues, it reverses its function and picks up carbon dioxide, the principal product of tissue respiration, for transport to the lungs, where it is expired. In this form, it is known as carboxyhaemoglobin and it is a purply-red colour.

The erythrocytes or red blood cells are ideally adapted for carrying oxygen. They contain haemoglobin, which gives them their red colour and is actively involved in oxygen transport. The shape of the cells means that they have a large surface area to volume ratio for the diffusion of gases, and having no nucleus means that there is the maximum amount of space available to pack in haemoglobin molecules. In fact, each red blood cell contains around 250 million molecules of haemoglobin, giving it the capacity to carry 1,000 million molecules of oxygen. To combine properly with oxygen, the red blood cells must contain adequate haemoglobin; this, in turn, depends on the amount of iron in the body. The organism derives its store of iron by absorption from the gut. The organism conserves and constantly reuses the supply of iron. A deficiency of haemoglobin caused by a lack of iron leads to anaemia.

II The Chemistry of Haemoglobin

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Haemoglobin is the key to oxygen uptake. It is a very large organic molecule made up of four globin polypeptide chains. Each chain has a prosthetic haem group which contains iron and gives the molecule its red colour. The shape of the protein chains and the way they are folded around the haem groups is vital to the way the molecule functions, and any changes in the chemistry of the blood that might affect the shape of these polypeptides could be lethal. Haemoglobin has a high affinity for oxygen—which means it takes up oxygen very readily. The oxygen is bound quite loosely to the haem groups to form oxyhaemoglobin.




Haemoglobin reacts with oxygen in a remarkable way. The first oxygen molecule to be attached alters the shape of the haemoglobin in such a way that it is easier for the next oxygen to be taken on. This in turn alters the shape and makes it easier for the next oxygen to be taken up, until the fourth and final oxygen molecule combines with the haemoglobin several hundred times more rapidly than the first. The same process happens in reverse when oxygen dissociates from haemoglobin: it becomes progressively harder to remove the oxygen. This has very important implications for the way in which oxygen is taken up in the lungs and released in the respiring cells.


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