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Published on March 15, 2014

Author: raniashok


PowerPoint Presentation: Mrs. Rani Ashok Associate Professor of Zoology, Lady Doak College, Madurai – 2 Email: RESPIRATORY PIGMENTS RESPIRATORY PIGMENTS: RESPIRATORY PIGMENTS Conjugated proteins Protein combines with metallic group which gives a characteristic colour on oxygenation Impart definite colour to the body fluids Functions of Respiratory Pigments: Functions of Respiratory Pigments Gas transport (O 2 and CO 2 ) Gas (O 2 ) storage pH buffers Enhancing gradients for gas diffusion Non-respiratory transport (e.g. NO) Possible enzymatic function (e.g., NO) HAEMOGLOBIN: HAEMOGLOBIN Widely distributed Vertebrates – seen in erythrocytes Invertebrates – dissolved in blood plasma Oxygen carrying capacity is high Efficient vehicle for oxygen transport Produced by liver cells Synthesized from acetic acid and glycine to form porphyrin which combines with iron to form haem molecule HAEMOGLOBIN …: HAEMOGLOBIN … Acetic acid + Glycine  Porphyrin Porphyrin + Iron  Haem Haem (4) + Globin (1)  haemoglobin HAEMOGLOBIN …: HAEMOGLOBIN … Colour of blood is due to haem In human – tetramer Molecular weight in corpuscles – 68,000 KDa Molecular weight in solution outside corpuscle – 6,000,000 KDa In Glycera and Notomatus – two monomer with molecular weight of 34,000 Kda Vertebrate haemoglobin differ in aminoacid composition, arrangement and in oxygen-binding characteristics Factors Affecting Affinity: Factors Affecting Affinity Specific variant of Hb Cooperativity of binding in multimeric forms Temperature pH Carbon Dioxide Organic Phosphates Inorganic Ions Complete the table by adding high or low to the blanks: Complete the table by adding high or low to the blanks Region of body Oxygen concentration Carbon dioxide concentration Affinity of haemoglobin for oxygen Result Gas exchange surface Oxygen is attached Respiring tissues Oxygen is released Affinity of haemoglobin under different conditions Affinity of haemoglobin under different conditions: Affinity of haemoglobin under different conditions Region of body Oxygen concentration Carbon dioxide concentration Affinity of haemoglobin for oxygen Result Gas exchange surface High Low High Oxygen is attached Respiring tissues Low High Low Oxygen is released MYOGLOBIN : MYOGLOBIN Iron- and oxygen-binding protein found in the muscle tissue of vertebrates in general and in almost all mammals Related to hemoglobin Found in the bloodstream is when it is released following muscle injury Abbreviated as Mb – single chain globular protein of 153 or 154 amino acids, containing a heme (iron containing porphyrin ) prosthetic group in the center around which the remaining apoprotein folds. Has eight alpha helices and a hydrophobic core. Has a molecular weight of 16,700 daltons MYOGLOBIN: MYOGLOBIN First protein to have its three-dimensional structure revealed Has an "instant binding tenacity" to oxygen given its hyperbolic oxygen dissociation curve. High concentrations of myoglobin in muscle cells allow organisms to hold their breaths longer. Diving mammals such as whales and seals have muscles with particularly high myoglobin abundance HAEMOCYANIN: HAEMOCYANIN Main non- haem respiratory pigment Wide occurrence Always present in colloidal solution Copper bearing protein Blue colour Found in two main Phyla of invertebrates – Mollusca and Arthropoda Molecular weight: Mollusca – 50,000 Kda Arthropoda – 74,000KDa Haemocyanin …: Haemocyanin … Combines with carbon monoxide Leaves carbon monoxide when in contact with air and regains its characteristic colour HAEMOERYTHRIN: HAEMOERYTHRIN Iron-bearing protein Molecular weight – 10,000 Kda Found in coelomocyte corpuscles and circulate with coelomic fluid Oxygenated: purple Deoxygenated: colourless Found only in few groups of animals CHLOROCRUORIN: CHLOROCRUORIN Oxygen-binding heme protein Seen in annelids – manly marine polychaetes Oxygen affinity is weaker than that of most haemoglobins Dichromatic comound Appears green in dilute solution and red in concentrated solution CHLOROCRUORIN: CHLOROCRUORIN Its structure is very similar to erythrocruorin (which is likewise very similar to multiple subunits of myoglobin ) Contains many 16-17 KDa myoglobin -like subunits arranged in a giant complex of over a hundred subunits with interlinking proteins as well with a total weight exceeding 3600 Kda Chlorocruorin carries an abnormal heme group structure Found free floating in the plasma, and not contained within red blood cells Thank You: Thank You

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