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Lecture 1

BIOB34H3 Lecture 1: 14

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Department
Biological Sciences
Course
BIOB34H3
Professor
Blake Richards
Semester
Fall

Description
12202015 OneNote Online O2 and CO2 Transport Tuesday, December 8, 2015 7:58 PM Fetal hemoglobin has a higher affinity for O whic2 means that itll automatically leave the mother and go to the fetus. Also, even if the partial pressure of O remains relatively low, the fetus can 2 become well oxygenated due to its high affinity for oxygen. Hemoglobins are one of several types of respiratory pigments or oxygentransport pigments. The defining property of respiratory pigments is that they undergo reversible combination with molecular oxygen (O ) 2 Although oxygen dissolves readily with the aqueous solution of blood plasma, its solubility is relatively low, so we need hemoglobin to increase the amount of O that can 2e carried by a unit of volume of blood. A respiratory pigment increases the oxygencarrying capacity of blood. The word hemoglobin refers to a family of many different compounds They also act as buffers and participate in blood CO trans2ort. When respiratory pigments combine with O , they are2said to be oxygenated and when they release O , they are said to be deoxygenated. 2 They are not said to be oxidized or reduced like most other molecules. The prefix oxy means oxygenated while deoxy means deoxygenated Respiratory pigments change colour when oxygenated or deoxygenated, and the measures of these colours can be used to monitor the oxygenation and deoxygenation of blood The binding of blood to haemoglobins occurs by noncovalent, weak bonding Haemoglobins have allosteric binding sites for allosteric ligands such as H and CO + 2 They are also multisubunit proteins Despite sharing many key properties with enzymes, however, the respiratory pigments differ from enzymes in a major way: They do not modify their primary ligand. They combine with oxygen and later release oxygen. Haemoglobins contain heme and are the most widespread respiratory pigments Heme is an iron thingy Globin is a protein which heme is noncovalently bonded to Oxygen heavydependent cells such as muscle fiber cells require additional monomeric (singleunit) muscle haemoglobins called myoglobins , the occur in the cytoplasm of muscle cells (especially abundant in cardiac muscle fibers). In humans, fetuses synthesize globin (as adults do) and globin, which differs from the globin synthesized by adults. The blood haemoglobins of vertebrates are always contained in specialized cells, the red blood cells (erythrocytes). Copperbased hemocyanins occur in many arthropods and molluscs Hemocyanins are found in just two phylathe arthropods and the molluscs. They rank as the second most common class of respiratory pigments Chlorocruorins, also sometimes called green haemoglobins, occur in just four families of marine annelid worms, including the fan worms and featherduster worms. Always found extracellularly, dissolved in blood plasma They are red in a concentrated solution, and green in a dilute one Hemerythrins have a distribution that is puzzling because it is both limited and farflung, encompassing three or four phyla. Despite their name, they dont contain any heme, they instead contain iron bound directly to the protein. https:adminmailutorontomy.sharepoint.compersonalhema_potluri_mail_utoronto_ca_layouts15WopiFrame.aspx?guestaccesstoken=0NXnTejTLtMMJI2 14
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