Erythrocytes take up carbon dioxide and release oxygen (Homo sapiens)

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<?xml version="1.0" encoding="UTF-8"?> <Pathway xmlns="http://pathvisio.org/GPML/2013a" Name="Erythrocytes take up carbon dioxide and release oxygen" Organism="Homo sapiens"> <Comment Source="WikiPathways-description">Carbon dioxide (CO2) in plasma is hydrated to yield protons (H+) and bicarbonate (HCO3-) by carbonic anhydrase IV (CA4) located on the apical plasma membranes of endothelial cells. Plasma CO2 is also taken up by erythrocytes via AQP1 and RhAG. Within erythrocytes CA1 and, predominantly, CA2 hydrate CO2 to HCO3- and protons (reviewed in Geers &amp; Gros 2000, Jensen 2004, Boron 2010). The HCO3- is transferred out of the erythrocyte by the band 3 anion exchange protein (AE1, SLC4A1) which cotransports a chloride ion (Cl-) into the erythrocyte.&lt;br&gt;Also within the erythrocyte, CO2 combines with the N-terminal alpha amino groups of HbA to form carbamates while protons bind histidine residues in HbA. The net result is the Bohr effect, a conformational change in HbA that reduces its affinity for O2 and hence assists the delivery of O2 to tissues. 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LineThickness="1.0"> <Point X="218.0" Y="658.0" GraphRef="c8133" RelX="0.9574468085106383" RelY="0.0" /> <Point X="312.0" Y="658.0" GraphRef="fe8bb" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-6806831" /> </Interaction> <Interaction GraphId="aa045"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="631.0" Y="214.0" GraphRef="c12dc" RelX="-1.0" RelY="0.0" /> <Point X="686.0" Y="259.0" GraphRef="f6ff7" RelX="-4.0" RelY="-0.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237038" /> </Interaction> <Interaction GraphId="aa1dc"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="418.0" Y="321.0" GraphRef="d326f" RelX="-1.0" RelY="0.0" /> <Point X="451.0" Y="372.0" GraphRef="ecaba" RelX="38.0" RelY="-10.5" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1475435" /> </Interaction> <Interaction GraphId="aaecb"> <Comment Source="Reactome">Carbonic anhydrase I (CA1, Khalifah 1971, Pesando 1975, Simonsson et al. 1982, Ren &amp; Lindskog 1992) and carbonic anhydrase II (CA2, Tibell et al. 1984, Jones &amp; Shaw 1983, Ghannam et al. 1986) hydrate carbon dioxide (CO2) to yield bicarbonate (HCO3-) and a proton (H+). During the reaction a hydroxyl group bound by the zinc ion (Zn2+) attacks the CO2 molecule in the active site to directly form HCO3- (reviewed in Lindskog 1997). The HCO3- is displaced by water, which is then deprotonated by a histidine residue to recreate the Zn2+:hydroxyl group. Depending on the concentrations of reactants the reaction is reversible.</Comment> <BiopaxRef>fa3</BiopaxRef> <BiopaxRef>ccd</BiopaxRef> <BiopaxRef>dc0</BiopaxRef> <BiopaxRef>bf5</BiopaxRef> <BiopaxRef>e2e</BiopaxRef> <BiopaxRef>d34</BiopaxRef> <BiopaxRef>d44</BiopaxRef> <BiopaxRef>a86</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="358.0" Y="352.0" /> <Point X="468.0" Y="413.0" /> <Anchor Position="0.0" Shape="None" GraphId="e40f4" /> <Anchor Position="0.99" Shape="None" GraphId="a9a5b" /> <Anchor Position="0.5" Shape="None" GraphId="ecaba" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1475435" /> </Interaction> <Interaction GraphId="b3802"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="182.0" Y="81.0" GraphRef="f7d8e" RelX="0.0" RelY="1.0" /> <Point X="183.0" Y="84.0" GraphRef="b233d" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237042" /> </Interaction> <Interaction GraphId="b4081"> <Comment Source="Reactome">Carbonic anhydrase IV (CA4) anchored to extracellular face of the plasma membrane (Wistrand et al. 1999) hydrates carbon dioxide (CO2) to yield bicarbonate (HCO3-) and a proton (H+) (Zhu &amp; Sly 1990, Okayuma et al. 1992, Baird et al. 1997, Innocenti et al. 2004). During the reaction a hydroxyl group bound by the zinc ion (Zn2+) of CA4 attacks the CO2 molecule to directly form HCO3- (reviewed in Lindskog 1997). The HCO3- is displaced by water, which is then deprotonated by a histidine residue to recreate the Zn2+:hydroxyl group. Depending on the concentrations of reactants the reaction is reversible.</Comment> <BiopaxRef>a31</BiopaxRef> <BiopaxRef>e59</BiopaxRef> <BiopaxRef>c47</BiopaxRef> <BiopaxRef>eff</BiopaxRef> <BiopaxRef>bf5</BiopaxRef> <BiopaxRef>f8c</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="385.0" Y="109.0" /> <Point X="451.0" Y="106.0" /> <Anchor Position="0.0" Shape="None" GraphId="cdfea" /> <Anchor Position="0.99" Shape="None" GraphId="c5a04" /> <Anchor Position="0.5" Shape="None" GraphId="cc0e0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237047" /> </Interaction> <Interaction GraphId="b4694"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="468.0" Y="413.0" GraphRef="a9a5b" RelX="1.1000000000000227" RelY="0.6100000000000136" /> <Point X="531.0" Y="429.0" GraphRef="db6c4" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1475435" /> </Interaction> <Interaction GraphId="b510c"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="451.0" Y="106.0" GraphRef="c5a04" RelX="0.6599999999999682" RelY="-0.030000000000001137" /> <Point X="809.0" Y="92.0" GraphRef="b6cea" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237047" /> </Interaction> <Interaction GraphId="b76b5"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="425.0" Y="658.0" GraphRef="bf469" RelX="1.1299999999999955" RelY="0.0" /> <Point X="442.0" Y="623.0" GraphRef="e588a" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-6806831" /> </Interaction> <Interaction GraphId="b8367"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="622.0" Y="494.0" GraphRef="d23b3" RelX="1.9200000000000728" RelY="0.01999999999998181" /> <Point X="716.0" Y="478.0" GraphRef="ad571" RelX="-1.0" RelY="0.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237325" /> </Interaction> <Interaction GraphId="b8e38"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="242.0" Y="228.0" GraphRef="c32bb" RelX="-1.0" RelY="0.0" /> <Point X="193.0" Y="230.0" GraphRef="ea2b9" RelX="7.0" RelY="2.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237042" /> </Interaction> <Interaction GraphId="c00b6"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="332.0" Y="604.0" GraphRef="fcf25" RelX="-1.0" RelY="0.0" /> <Point X="360.0" Y="658.0" GraphRef="cd4c9" RelX="-8.5" RelY="0.0" ArrowHead="mim-catalysis" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-6806831" /> </Interaction> <Interaction GraphId="c4949"> <Comment Source="Reactome">The Bohr effect refers to the observation that carbon dioxide (CO2) decreases the affinity of hemoglobin (HbA) for oxygen (O2) (Rossi-Bernardi &amp; Roughton 1967, Kwant et al. 1988, Dash &amp; Bassingthwaighte 2010). The Bohr effect has two components: protonation of histidines in HbA (Chatake et al. 2007, Kovalevsky et al. 2010, Fang et al. 1999) and chemical reaction (carbamation) of the N-terminal valines of HbA by CO2 (Ferguson &amp; Roughton 1934, Forster et al. 1968, Bauer &amp; Schroder 1972, Morrow et al. 1973, Morrow et al. 1976, Mathew et al. 1977, Acharya et al. 1994). The protons (H+) for this reaction are produced by carbonic anhydrase acting on water and CO2 to produce bicarbonate (HCO3-) and H+ (Kernohan &amp; Roughton 1968).</Comment> <BiopaxRef>b7e</BiopaxRef> <BiopaxRef>c9d</BiopaxRef> <BiopaxRef>aad</BiopaxRef> <BiopaxRef>a23</BiopaxRef> <BiopaxRef>cf5</BiopaxRef> <BiopaxRef>f42</BiopaxRef> <BiopaxRef>da7</BiopaxRef> <BiopaxRef>a18</BiopaxRef> <BiopaxRef>fc8</BiopaxRef> <BiopaxRef>a4b</BiopaxRef> <BiopaxRef>cd6</BiopaxRef> <BiopaxRef>a5e</BiopaxRef> <BiopaxRef>f58</BiopaxRef> <BiopaxRef>ce5</BiopaxRef> <BiopaxRef>acf</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="430.0" Y="492.0" /> <Point X="622.0" Y="494.0" /> <Anchor Position="0.0" Shape="None" GraphId="d71c2" /> <Anchor Position="0.99" Shape="None" GraphId="d23b3" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237325" /> </Interaction> <Interaction GraphId="c63bf"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="277.0" Y="550.0" GraphRef="e1ac4" RelX="1.0" RelY="0.0" /> <Point X="430.0" Y="492.0" GraphRef="d71c2" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237325" /> </Interaction> <Interaction GraphId="c9c09"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="550.0" Y="149.0" GraphRef="b1e67" RelX="0.9428571428571428" RelY="0.0" /> <Point X="645.0" Y="260.0" GraphRef="b84f4" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237038" /> </Interaction> <Interaction GraphId="cec0e"> <Comment Source="Reactome">The band 3 anion exchange protein (AE1, SLC4A1) exchanges chloride (Cl-) for bicarbonate (HCO3-) across the plasma membrane according to the concentration gradients of the anions (Knauf et al. 1996, Dahl et al. 2003). SLC4A1 may be part of a complex ("metabolon") with carbonic anhydrase II (CA2) which would facilitate the transport of HCO3- (Sterling et al. 2001).</Comment> <BiopaxRef>bbc</BiopaxRef> <BiopaxRef>f4e</BiopaxRef> <BiopaxRef>fb7</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="645.0" Y="260.0" /> <Point X="735.0" Y="259.0" /> <Anchor Position="0.0" Shape="None" GraphId="b84f4" /> <Anchor Position="0.99" Shape="None" GraphId="a9109" /> <Anchor Position="0.5" Shape="None" GraphId="f6ff7" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237038" /> </Interaction> <Interaction GraphId="d1498"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="189.0" Y="372.0" GraphRef="a5856" RelX="0.060000000000002274" RelY="2.8799999999999955" /> <Point X="189.0" Y="375.0" GraphRef="f94d9" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237042" /> </Interaction> <Interaction GraphId="d2a8e"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="187.0" Y="372.0" GraphRef="b8ee0" RelX="0.060000000000002274" RelY="2.8799999999999955" /> <Point X="189.0" Y="375.0" GraphRef="f94d9" RelX="0.0" RelY="-1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237069" /> </Interaction> <Interaction GraphId="d2d59"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="276.0" Y="706.0" GraphRef="c856a" RelX="1.0" RelY="0.0" /> <Point X="312.0" Y="658.0" GraphRef="fe8bb" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-6806831" /> </Interaction> <Interaction GraphId="d7bfe"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="409.0" Y="449.0" GraphRef="ba52a" RelX="-0.02857142857142857" RelY="1.0" /> <Point X="430.0" Y="492.0" GraphRef="d71c2" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237325" /> </Interaction> <Interaction GraphId="d8536"> <Comment Source="Reactome">Aquaporin-1 (AQP1) passively transports carbon dioxide (CO2) across the plasma membrane according to the concentration gradient (Nakhoul et al. 1998, Blank &amp; Ehmke et al. 2003, Endeward et al. 2006, Musa-Aziz et al. 2009). The pore in AQP1 that conducts CO2 may be distinct from the pore that conducts water.</Comment> <BiopaxRef>b0c</BiopaxRef> <BiopaxRef>be2</BiopaxRef> <BiopaxRef>bab</BiopaxRef> <BiopaxRef>d8d</BiopaxRef> <BiopaxRef>e7f</BiopaxRef> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="183.0" Y="84.0" /> <Point X="189.0" Y="372.0" /> <Anchor Position="0.0" Shape="None" GraphId="b233d" /> <Anchor Position="0.99" Shape="None" GraphId="a5856" /> <Anchor Position="0.5" Shape="None" GraphId="ea2b9" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237042" /> </Interaction> <Interaction GraphId="db9ab"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="336.0" Y="142.0" GraphRef="dc2eb" RelX="1.0" RelY="0.0" /> <Point X="385.0" Y="109.0" GraphRef="cdfea" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237047" /> </Interaction> <Interaction GraphId="e0ec2"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="182.0" Y="81.0" GraphRef="f7d8e" RelX="0.0" RelY="1.0" /> <Point X="181.0" Y="84.0" GraphRef="b363c" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237069" /> </Interaction> <Interaction GraphId="e3e22"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="330.0" Y="324.0" GraphRef="c080d" RelX="0.0" RelY="1.0" /> <Point X="358.0" Y="352.0" GraphRef="e40f4" RelX="0.0" RelY="0.0" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1475435" /> </Interaction> <Interaction GraphId="e4b60"> <Graphics ConnectorType="Segmented" ZOrder="12288" LineThickness="1.0"> <Point X="735.0" Y="259.0" GraphRef="a9109" RelX="0.8999999999999773" RelY="-0.009999999999990905" /> <Point X="836.0" Y="107.0" GraphRef="b6cea" RelX="-0.01818181818181818" RelY="1.0" ArrowHead="Arrow" /> </Graphics> <Xref Database="Reactome" ID="R-HSA-1237038" /> </Interaction> <Interaction GraphId="e8b22"> <Comment Source="Reactome">NADH-Cytochrome b5 reductases (CYB5Rs), flavoproteins consisting of NADH and flavin adenine dinucleotide (FAD) binding domains, catalyse electron transfer from the two-electron carrier NADH to the one-electron carrier ferricytochrome b5 ((Fe(3+)Cb5), forming ferrocytochrome b5 ((Fe(2+)Cb5) (Zhu et al. 1999, Baker et al. 2005, Zhu et al. 2004). CYB5Rs participate in fatty acid synthesis, cholesterol synthesis and xenobiotic oxidation as members of the electron transport chain on the endoplasmic reticulum membrane. 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basis of the Bohr effect and of beta 143 histidine in the binding of 2,3-bisphosphoglycerate in human normal adult hemoglobin.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Fang TY, Zou M, Simplaceanu V, Ho NT, Ho C.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="b0c"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">12754312</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Aquaporin-1 and HCO3(-)-Cl- transporter-mediated transport of CO2 across the human erythrocyte membrane.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Blank ME, Ehmke H.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" 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Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Sterling D, Reithmeier RA, Casey JR.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="acf"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">5656372</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Reaction of CO2 with human hemoglobin solution.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Forster RE, Constantine HP, Craw MR, Rotman HH, Klocke RA.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="ec0"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">11034202</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Structural determinants of water permeation through aquaporin-1.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Murata K, Mitsuoka K, Hirai T, Walz T, Agre P, Heymann JB, Engel A, Fujiyoshi Y.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="e7c"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">10096900</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Hydrodynamic properties of human erythrocyte band 3 solubilized in reduced Triton X-100.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Taylor AM, Boulter J, Harding SE, Cölfen H, Watts A.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="ad6"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">7742555</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Association state of human red blood cell band 3 and its interaction with ankyrin.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pinder JC, Pekrun A, Maggs AM, Brain AP, Gratzer WB.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="d36"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">9253766</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Gel filtration chromatographic studies of the isolated membrane domain of band 3.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Salhany JM, Cordes KA, Sloan RL.</bp:AUTHORS> </bp:PublicationXref> <bp:PublicationXref xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:id="a5e"> <bp:ID rdf:datatype="http://www.w3.org/2001/XMLSchema#string">20162361</bp:ID> <bp:DB rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PubMed</bp:DB> <bp:TITLE rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Erratum to: Blood HbO2 and HbCO2 dissociation curves at varied O2, CO2, pH, 2,3-DPG and temperature levels.</bp:TITLE> <bp:AUTHORS rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Dash RK, Bassingthwaighte JB.</bp:AUTHORS> </bp:PublicationXref> <bp:openControlledVocabulary xmlns:bp="http://www.biopax.org/release/biopax-level3.owl#"> <bp:TERM xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:datatype="http://www.w3.org/2001/XMLSchema#string">classic metabolic pathway</bp:TERM> <bp:ID xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:datatype="http://www.w3.org/2001/XMLSchema#string">PW:0000002</bp:ID> <bp:Ontology xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" rdf:datatype="http://www.w3.org/2001/XMLSchema#string">Pathway Ontology</bp:Ontology> </bp:openControlledVocabulary> </Biopax> </Pathway>

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