BIOL 460 1st Edition Lecture 29Outline of Last Lecture I. Starling’s ForcesII. Regulation of Breathing III. Chemoreceptors a. centralb. peripheralc. Hypoventilation d. HyperventilationOutline of Current Lecture I. Hemoglobin and O2 TransportII. CO2 TransportIII. Acid-base BalanceCurrent Lecture1. Hemoglobin and O2 transporta. Hemoglobini. 4 polypeptidesii. Globin – proteiniii. Hemo – heme group (porphorin ring with iron in center)iv. Iron forms covalent bond with O2b. Oxyhemoglobin – hemoglobin + O2c. Deoxyhemoglobin – hemoglobin onlyd. Deoxyhemoglobin + O2 oxyhemoglobine. CO – carboxyhemoglobini. Bond is 200x greater than O2ii. Treat by putting poisoned individual in hyperbaric O2 changeThese notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.f. Two factors determine shift of reactioni. ppO2ii. Bond affinity (strength between O2 and heme group)g. % oxyhemoglobin saturation tells how much hemoglobin is oxyhemoglobini. Normal – 97%ii. Use arterial bloodiii. Spectrophotometer – redder = more hemoglobiniv. Pulse oximeter – shines 2 lights into blood and determines how much of each wavelength is absorbed, algorithm uses this info to determine how much hemoglobin is bonded to O2 (occurs with pulse rate)h. O2 carrying capacity in blood determined by [hemoglobin]i. Anemia – less O2 than normal because of lack of hemoglobinii. Polycythemia – more hemoglobin in blood than normaliii. Kidneys determine how much hemoglobin is in blood1. Secrete erythropoietin2. Bone marrow produces more RBCsi. Loading reactioni. Higher ppO2ii. Stronger bond affinityj. Unloading reactioni. Lower ppO2ii. Weaker bond affinityk. Oxyhemoglobin dissociation curve (see notes) – 16.33i. S shapedii. Flat at high and low ppO2iii. Exercise drops ppO2 slightlyl. Bond affinityi. Affected by pHii. Bohr effectiii. Temperature – higher = weaker bondiv. Happens during exercise as wellm. 2,3 bisphosphoglyceratei. Erythrocytes have no mitochondriaii. Only make ATP through fermentationiii. 1,3 bisphosphoglycerate 2,3 bisphosphoglycerate mutase 2,3 bisphosphoglycerateiv. shift to right, bond affinity is weakenedv. produced with anemia or if someone moves to a high altitude less oxyhemoglobin1. oxyhemoglobin inhibits 2,3 bisphosphoglycerate mutase2. no OHb to inhibit with anemia or altitude change2. CO2 Transporta. 10% dissolved in plasmab. 20% bonds to globin of hemoglobin, producing carbaminohemoglobinc. 70% transported as bicarbonated. RBCs contain carbonic anhydrasei. Accelerates rxnii. CO2 + H2O H2CO3 H+ + HCO3-iii. Can accelerate in either directioniv. Protons combine with globin part of hemoglobin, enhancing Bohr effectv. HCO3- exits RBC, CL- enters (chloride shif)vi. Everything is reversed exactly when CO2 reaches lungs3. Acid-base balancea. pH of blood of arterial plasma= 7.35-7.45i. deviation is serious and can interfere with enzyme activity ii. lower pH= acidosisiii. higher pH= alkalosis b. Carbonic acid (H2CO3)-i. volatile acid b/c if reversed it can be a converted into gas c. Other acidsi. Metabolic acids- non-volatile 1. Can’t be converted into
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