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Biology Presentation (Mrs. Booth) - Hemoglobin
Transcript of Biology Presentation (Mrs. Booth) - Hemoglobin
- Red Blood Cells
- White Blood Cells
- Platelets "Red Blood Cells are so numerous because they perform the most essential function of blood." all red blood cells are produced in red bone marrow they are the spongy tissue on the bulbous ends of long bones and at the centre of flat bones e.g hips and ribs. 1 In the marrow, red blood cells start out as undifferentiated stem cells called "hemoctoblasts" 2 If the body detects a minuscule drop in oxygen carrying capacity, Erythropoietin is released from the kidney that triggers the stem cells to become red blood cells.how haemoglobin works is actually a bi product of allosteric inhibition (usually associated with enzymes) - binding to other parts of protein to affect the ability of the enzyme to do what it normally does. 3 Because red blood cells only live 120 days, the supply must be continuously replenished - roughly 2million RBC are born every second. 4 A mature red blood cell has no nucleus. The nucleus is split out during the final stages of the cell's two day development before taking a biconcave shape. Now the Question is... How can RBC transport oxygen? Like all cells, red blood cells are mostly water, but 97% of their solid matter is "HAEMOGLOBIN". Haemoglobin is an iron-containing protein in the red blood cells. Haemoglobin carries oxygen around the body and without enough of it your muscles and organs don't get all the oxygen they need. Females Males (cc) image by anemoneprojectors on Flickr 115-165 g/L 125 - 185 g/L Blood Service Haemoglobin reference range What is a normal haemoglobin level? Haemoglobin protein is made up of four amino acid chains. "curly ribbons" - 2 red & 2 blues as seen above. e.g. moving leg so co2 produced and so just haeomo comes by and let goes of it o2 and joins with co2
co2 --> disassociate to carbonic acid and disassocoate so give H+ redblood cells ar 25% bigger than the largest capplaries so it squeases the rbc and inorder that the pressure increase and and so it releases o2 from the hemoglobin In each ribbon, there is a "Heme" group (Green), which has a porphyrin structure The key is the Fe in the middle of the structure where it is able to hold and release oxygen and transport them through out the body. Interestingly, instead of Fe ion in the middle of the structure, plant cells have a Mg ion where it helps chlorophyll to absorb UV light. How haemoglobin can attract oxygen is actually a really amazing process - which is called "Co-operative Binding". In simple terms: Co-operative binding is once one haemoglobin protein binds with one oxygen, it sets out a chain reaction where all the active sites of the other haemoglobin will change their shapes so that it would increase the probability of binding with oxygen.
So even simpler: it makes it an oxygen acceptor. Now we know how haemoglobin gets oxygen, but the true question is - how do they know when to dump them??? How haemoglobin works is actually a bi-product of allosteric inhibition (usually associated with enzymes) - which is binding to other parts of protein to affect the ability of the enzyme from what it normally does. So... Haemoglobin is allosteric inhibited by carbon dioxide and protons which means both carbon dioxide and proton can bind with other parts of the haemoglobin. For an example, during exercise, your leg muscles cells produce a lot of carbon dioxide due to respiration for the release of energy. The carbon dioxide from the cells will diffuse out into the capillaries and react with water to form carbonic acid.
Remember: 54% of plasma is water And remember we talked about protons can allistericly inhibit haemoglobin?
Protons are actually hydrogen ions which can be disassociated from the carbonic acid in the capillaries. High % of protons = High in acidity When the blood has a relavtively higher acidity, it allosterically inhibits the hemoglobin's active sites to change shape and because of that they
cannot hold on to the oxygen as well as before and release them. And thanks to co-operation bonding, this process is spread out, and acts like a signal to the haemoglobin for when the oxygen should be released and when carbon dioxide should be taken in. This is a brilliant mechanism as our haemoglobin protein can tell when to deposit the oxygen and when to take in carbon dioxide. Extra fact: RBCs are actually 25% larger than the largest capillaries and that is believed that it increases the pressure so that oxygen can be squeezed out from the haemoglobin. Still don't get it? Here's an easier explanation - a diagram! And... in order to thank you for your lovely patience of reading through this grueling piece of project... ... here's a 2 minute movie for you to enjoy! Where did they put Dracula when he was arrested?
. . . In a red blood cell! End of the line after 120 days... And the process starts all over again... Specialised white blood cells in the liver and spleen called Kupffer cells prey on dying RBCs, ingesting them whole and breaking them down into reusable components. The divorce... In the belly of the Kupffer cells, haemoglobin molecules are split into heme and globin.
Heme is broken down further into bile and Fe ions which some are carried back and stored in the bone marrow.
Globin and other cellular membranes are converted back into basic amino acids, some will be used again to re-create red blood cells.