382:
increases until the maximum amount that can be bound is reached. As this limit is approached, very little additional binding occurs and the curve levels out as the hemoglobin becomes saturated with oxygen. Hence the curve has a sigmoidal or S-shape. At pressures above about 60 mmHg, the standard dissociation curve is relatively flat, which means that the oxygen content of the blood does not change significantly even with large increases in the oxygen partial pressure. To get more oxygen to the tissue would require blood transfusions to increase the hemoglobin count (and hence the oxygen-carrying capacity), or supplemental oxygen that would increase the oxygen dissolved in plasma. Although binding of oxygen to hemoglobin continues to some extent for pressures about 50 mmHg, as oxygen partial pressures decrease in this steep area of the curve, the oxygen is unloaded to peripheral tissue readily as the hemoglobin's affinity diminishes. The partial pressure of oxygen in the blood at which the hemoglobin is 50% saturated, typically about 26.6 mmHg (3.5 kPa) for a healthy person, is known as the
294:
961:
36:
191:
128:
285:, the partial pressure of oxygen is typically high, and therefore the oxygen binds readily to hemoglobin that is present. As the blood circulates to other body tissue in which the partial pressure of oxygen is less, the hemoglobin releases the oxygen into the tissue because the hemoglobin cannot maintain its full bound capacity of oxygen in the presence of lower oxygen partial pressures.
277:. Expressed as a percentage, the oxygen saturation is the ratio of the amount of oxygen bound to the hemoglobin, to the oxygen-carrying capacity of the hemoglobin. The oxygen-carrying capacity of hemoglobin is determined by the type of hemoglobin present in the blood. The amount of oxygen bound to the hemoglobin at any time is related, in large part, to the
440:
to oxygen (requiring a higher partial pressure of oxygen to achieve the same oxygen saturation), but it makes it easier for the hemoglobin to release oxygen bound to it. The effect of this shift of the curve increases the partial pressure of oxygen in the tissues when it is most needed, such as during exercise, or hemorrhagic shock.
975:(HbA), giving HbF a higher affinity for oxygen than HbA. HbF is composed of two alpha and two gamma chains whereas HbA is composed of two alpha and two beta chains. The fetal dissociation curve is shifted to the left relative to the curve for the normal adult because of these structural differences:
995:
formed, and 2,3-BPG binds readily to beta chains rather than to alpha chains. As a result, 2,3-BPG binds more strongly to adult hemoglobin, causing HbA to release more oxygen for uptake by the fetus, whose HbF is unaffected by the 2,3-BPG. HbF then delivers that bound oxygen to tissues that have even
776:
Increase in temperature shifts the oxygen dissociation curve to the right. When temperature is increased keeping the oxygen concentration constant, oxygen saturation decreases as the bond between oxygen and iron gets denatured. Additionally, with increased temperature, the partial pressure of oxygen
439:
The strength with which oxygen binds to hemoglobin is affected by several factors. These factors shift or reshape the oxyhemoglobin dissociation curve. A shift to right indicates that the hemoglobin under study has a decreased affinity for oxygen. This makes it more difficult for hemoglobin to bind
872:
state. This causes a leftward shift in the oxygen hemoglobin dissociation curve, as any residual heme with oxygenated ferrous iron (+2 state) is unable to unload its bound oxygen into tissues (because 3+ iron impairs hemoglobin's cooperativity), thereby increasing its affinity with oxygen. However,
381:
In its simplest form, the oxyhemoglobin dissociation curve describes the relation between the partial pressure of oxygen (x axis) and the oxygen saturation (y axis). Hemoglobin's affinity for oxygen increases as successive molecules of oxygen bind. More molecules bind as the oxygen partial pressure
700:
content of blood is transported as carbamino compounds, whereas (80–90%) is transported as bicarbonate ions and a small amount is dissolved in the plasma. The formation of a bicarbonate ion will release a proton into the plasma, decreasing pH (increased acidity), which also shifts the curve to the
978:
In adult hemoglobin, the binding of 2,3-bisphosphoglycerate (2,3-BPG) primarily occurs with the beta chains, preventing the binding of oxygen with haemoglobin. This binding is crucial for stabilizing the deoxygenated state of hemoglobin, promoting the efficient release of oxygen to body tissues.
842:; the binding of the carbon monoxide to the iron centre of hemoglobin is much stronger than that of oxygen, and the binding site remains blocked for the remainder of the life cycle of that affected red blood cell. With an increased level of carbon monoxide, a person can suffer from severe tissue
640:
ion concentration, various amino acid residues, such as
Histidine 146 exist predominantly in their protonated form allowing them to form ion pairs that stabilize deoxyhemoglobin in the T state. The T state has a lower affinity for oxygen than the R state, so with increased acidity, the hemoglobin
235:
of the blood changes; this causes another change in the shape of hemoglobin, which increases its ability to bind carbon dioxide and decreases its ability to bind oxygen. With the loss of the first oxygen molecule, and the binding of the first carbon dioxide molecule, yet another change in shape
377:
The shape of the curve results from the interaction of bound oxygen molecules with incoming molecules. The binding of the first molecule is difficult. However, this facilitates the binding of the second, third and fourth, this is due to the induced conformational change in the structure of the
982:
In fetal hemoglobin, which possesses a gamma chain instead of a beta chain, the interaction with 2,3-BPG differes because 2,3 - -BPG not binds with gamma chain as it has lower to no affinity with gamma chain.This distinction contributes to fetal hemoglobin having a higher affinity for oxygen.
617:
emperature. Factors that move the oxygen dissociation curve to the right are those physiological states where tissues need more oxygen. For example, during exercise, muscles have a higher metabolic rate, and consequently need more oxygen, produce more carbon dioxide and lactic acid, and their
767:
of hemoglobin, lowering hemoglobin's affinity for oxygen by binding preferentially to deoxyhemoglobin. An increased concentration of BPG in red blood cells favours formation of the T (taut or tense), low-affinity state of hemoglobin and so the oxygen-binding curve will shift to the right.
777:
increases as well. So, one will have a lesser amount of hemoglobin saturated for the same oxygen concentration but at a higher partial pressure of oxygen. Thus, any point in the curve will shift rightwards (due to increased partial pressure of oxygen) and downwards (due to weakened
446:
This shift indicates that the hemoglobin under study has an increased affinity for oxygen so that hemoglobin binds oxygen more easily, but unloads it more reluctantly. Left shift of the curve is a sign of hemoglobin's increased affinity for oxygen (e.g. at the lungs).
829:
210 times more readily than with oxygen. Because of this higher affinity of hemoglobin for carbon monoxide than for oxygen, carbon monoxide is a highly successful competitor that will displace oxygen even at minuscule partial pressures. The reaction
986:
Typically, fetal arterial oxygen pressures are lower than adult arterial oxygen pressures. Hence higher affinity to bind oxygen is required at lower levels of partial pressure in the fetus to allow diffusion of oxygen across the
755:, among others, which necessitate easier oxygen unloading in the peripheral tissue. High levels of 2,3-BPG shift the curve to the right (as in childhood), while low levels of 2,3-BPG cause a leftward shift, seen in states such as
709:. This is a physiologically favored mechanism, since hemoglobin will drop off more oxygen as the concentration of carbon dioxide increases dramatically where tissue respiration is happening rapidly and oxygen is in need.
393:
is a conventional measure of hemoglobin affinity for oxygen. In the presence of disease or other conditions that change the hemoglobin oxygen affinity and, consequently, shift the curve to the right or left, the
236:
occurs, which further decreases the ability to bind oxygen, and increases the ability to bind carbon dioxide. The oxygen bound to the hemoglobin is released into the blood's plasma and absorbed into the
402:
indicates a rightward shift of the standard curve, which means that a larger partial pressure is necessary to maintain a 50% oxygen saturation. This indicates a decreased affinity. Conversely, a lower P
228:, it has the unbound conformation (shape). The binding of the first oxygen molecule induces change in the shape of the hemoglobin that increases its ability to bind to the other three oxygen molecules.
369:
247:
the reverse of this process takes place. With the loss of the first carbon dioxide molecule the shape again changes and makes it easier to release the other three carbon dioxides.
187:), and is determined by what is called "hemoglobin affinity for oxygen"; that is, how readily hemoglobin acquires and releases oxygen molecules into the fluid that surrounds it.
739:. The production of 2,3-BPG is likely an important adaptive mechanism, because the production increases for several conditions in the presence of diminished peripheral tissue O
165:
on the horizontal axis. This curve is an important tool for understanding how our blood carries and releases oxygen. Specifically, the oxyhemoglobin dissociation curve relates
815:
409:
The 'plateau' portion of the oxyhemoglobin dissociation curve is the range that exists at the pulmonary capillaries (minimal reduction of oxygen transported until the p(O
423:
To see the relative affinities of each successive oxygen as you remove/add oxygen from/to the hemoglobin from the curve compare the relative increase/decrease in p(O
696:
due to formation of bicarbonate ion. Formation of carbaminohemoglobin stabilizes T state hemoglobin by formation of ion pairs. Only about 5–10% of the total CO
897:, promoting the cellular supply of oxygen, and the addition of an iron salt provides for competitive binding of the free cyanide as the biochemically inert
107:
17:
653:. A reduction in the total binding capacity of hemoglobin to oxygen (i.e. shifting the curve down, not just to the right) due to reduced pH is called the
1228:
79:
416:
The 'steep' portion of the oxyhemoglobin dissociation curve is the range that exists at the systemic capillaries (a small drop in systemic capillary p(O
46:
913:
the kidneys. Methemoglobin is also formed in small quantities when the dissociation of oxyhemoglobin results in the formation of methemoglobin and
86:
1340:
1289:
1069:
93:
75:
214:. Each hemoglobin molecule has the capacity to carry four oxygen molecules. These molecules of oxygen bind to the globin chain of the
633:
ion concentration) shifts the standard curve to the right, while an increase shifts it to the left. This occurs because at greater
1268:
1186:
450:
Similarly, right shift shows decreased affinity, as would appear with an increase in either body temperature, hydrogen ions,
1333:
1088:
100:
1777:
1632:
1238:
705:
levels in the blood stream results in a high pH, and thus provides more optimal binding conditions for hemoglobin and O
723:
2,3-Bisphosphoglycerate or 2,3-BPG (formerly named 2,3-diphosphoglycerate or 2,3-DPG) is an organophosphate formed in
61:
65:
282:
1815:
1326:
311:
1696:
1211:
937:
270:
is produced, oxygen bound to the hemoglobin is released into the blood's plasma and absorbed into the tissues.
889:) can be used to deliberately oxidise hemoglobin and raise methemoglobin levels, restoring the functioning of
1423:
1545:
1820:
1715:
1664:
1515:
992:
736:
718:
578:
490:
451:
1669:
1297:
1577:
1508:
1489:
952:. The effects appear to last roughly as long as the affected red blood cells remain in circulation.
54:
1653:
1520:
1484:
1378:
752:
780:
1686:
1555:
50:
1503:
1450:
1440:
1349:
1691:
1627:
898:
764:
948:
of hemoglobin within red blood cells. It is an experimental drug intended to reduce tissue
420:) can result in the release of large amounts of oxygen for the metabolically active cells).
1746:
1601:
1565:
1400:
1395:
945:
926:
763:. In the absence of 2,3-BPG, hemoglobin's affinity for oxygen increases. 2,3-BPG acts as a
689:
1304:
680:
compounds to be generated through chemical interactions, which bind to hemoglobin forming
8:
1825:
1428:
922:
681:
154:
1756:
1751:
1731:
1589:
1465:
1005:
941:
890:
692:
as the inhibition happens not at the binding site of hemoglobin. Second, it influences
637:
630:
383:
1314:, pH and temperature on the oxygen–hemoglobin dissociation curve (left or right shift)
1794:
1710:
1676:
1478:
1433:
1415:
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1234:
1207:
1182:
949:
878:
858:
843:
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760:
274:
166:
162:
443:
In contrast, the curve is shifted to the left by the opposite of these conditions.
293:
1611:
1560:
1470:
1385:
968:
868:(the normal form, which on binding with oxygen changes to the ferric state) to the
693:
374:
A hemoglobin molecule can bind up to four oxygen molecules in a reversible method.
302:
278:
237:
218:
177:
944:
that causes a rightward shift in the oxygen hemoglobin dissociation curve through
861:
is a form of abnormal hemoglobin where the iron centre has been oxidised from the
1830:
1789:
1637:
1606:
865:
826:
161:
in its saturated (oxygen-laden) form on the vertical axis against the prevailing
1735:
1725:
1582:
1540:
1405:
732:
724:
669:
267:
255:
225:
925:
and causes biochemical damage, but is neutralised by the action of the enzyme
1809:
1741:
1497:
1410:
259:
1681:
1550:
1532:
1390:
1309:
972:
886:
756:
251:
1263:. North America: Lippincott, Williams, and Wilkins. 2007. pp. 24–35.
577:
affinity than adult hemoglobin; primarily due to much-reduced affinity to
27:
Visual tool used to understand how human blood carries and releases oxygen
1720:
1318:
1010:
960:
906:
902:
894:
654:
650:
273:
How much of that capacity is filled by oxygen at any time is called the
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203:
158:
64:
if you can. Unsourced or poorly sourced material may be challenged and
434:
1658:
869:
744:
677:
263:
657:. This is seen in bony fish. The binding affinity of hemoglobin to O
240:, and the carbon dioxide in the tissues is bound to the hemoglobin.
988:
586:
281:
of oxygen to which the hemoglobin is exposed. In the lungs, at the
378:
hemoglobin molecule induced by the binding of an oxygen molecule.
882:
874:
862:
190:
850:
because carboxyhemoglobin does not carry oxygen to the tissues.
1363:
1162:
Ahern, Kevin; Rajagopal, Indira; Tan, Taralyn (5 August 2017).
1147:
Ahern, Kevin; Rajagopal, Indira; Tan, Taralyn (5 August 2017).
748:
207:
244:
211:
1760:
1459:
838:
almost irreversibly displaces the oxygen molecules forming
511:
215:
1179:
Clinical
Chemistry: Fundamentals And Laboratory Techniques
254:, but to a much lesser degree. Hemoglobin is contained in
1261:
Lippincott's
Illustrated Review: Biochemistry 4th edition
803:
585:
The causes of shift to right can be remembered using the
454:(2,3-BPG) concentration or carbon dioxide concentration.
881:. In cases of accidental ingestion, administration of a
991:. At the placenta, there is a higher concentration of
427:) needed for the corresponding increase/decrease in s(O
232:
1068:
Ahern, Kevin; Rajagopal, Indira; Tan, Taralyn (2017).
901:
ion, . An alternative approach involves administering
783:
314:
435:
Factors that affect the standard dissociation curve
996:lower partial pressures where it can be released.
809:
406:indicates a leftward shift and a higher affinity.
363:
1166:(1.2 ed.). NC-Creative Commons. p. 134.
1161:
1151:(1.2 ed.). NC-Creative Commons. p. 370.
1146:
1067:
921:, instead of the usual products. Superoxide is a
231:In the presence of dissolved carbon dioxide, the
1807:
1305:The Interactive Oxyhemoglobin Dissociation Curve
1233:(8th ed.). Cengage Learning. p. 1032.
853:
817:bond), hence, the rightward shift of the curve.
250:Oxygen is also carried dissolved in the blood's
1201:
224:When hemoglobin has no bound oxygen, nor bound
1181:. St. Louis, Missouri: Elsevier. p. 226.
877:, and is therefore useful in the treatment of
60:Please review the contents of the article and
1334:
1204:Animal Physiology: Adaptation and Environment
206:(Hb) is the primary vehicle for transporting
971:(HbF) is structurally different from normal
262:is present, as it is in the tissues. In the
258:. Hemoglobin releases the bound oxygen when
1253:
1107:
1105:
364:{\displaystyle S(t)={\frac {1}{1+e^{-t}}}.}
1348:
1341:
1327:
1047:lyceric acid, an obsolete name for 2,3-BPG
1127:
1125:
1123:
873:methemoglobin has increased affinity for
301:The curve is usually best described by a
1102:
959:
672:affects the curve in two ways. First, CO
661:is greatest under a relatively high pH.
292:
189:
1131:
14:
1808:
1120:
76:"Oxygen–hemoglobin dissociation curve"
1322:
1176:
1111:
1077:(1.2 ed.). NC: Creative Commons.
940:(ITPP), also known as OXY111A, is an
1707:oxygen–hemoglobin dissociation curve
1226:
139:oxygen–hemoglobin dissociation curve
29:
18:Oxygen-hemoglobin dissociation curve
955:
649:(and more H). This is known as the
398:changes accordingly. An increased P
305:plot, using a formula of the kind:
24:
1633:hypoxic pulmonary vasoconstriction
1081:
1029:2,3-DPG is an abbreviation of 2,3-
1023:
932:
820:
25:
1842:
1287:
1281:
1230:Chemistry and Chemical Reactivity
964:Fetal hemoglobin saturation curve
664:
1136:. McGraw-Hill. pp. 156–175.
905:, thereby converting cyanide to
701:right as discussed above; low CO
288:
143:oxyhemoglobin dissociation curve
126:
34:
1310:Simulation of the parameters CO
1220:
1294:Essentials of Human Physiology
1206:. Cambridge University Press.
1195:
1170:
1155:
1140:
1061:
938:Myo-inositol trispyrophosphate
771:
626:A decrease in pH (increase in
324:
318:
62:add the appropriate references
13:
1:
1054:
893:. The nitrite also acts as a
854:Effects of methemoglobinaemia
846:while maintaining a normal pO
810:{\displaystyle {\ce {Hb-O2}}}
573:fetal hemoglobin has higher O
198:
157:that plots the proportion of
1116:(6th ed.). p. 169.
283:alveolar–capillary interface
7:
1665:Ventilation/perfusion ratio
1516:pulmonary stretch receptors
999:
737:2,3-bisphosphoglyceric acid
719:2,3-bisphosphoglyceric acid
456:
297:Hemoglobin saturation curve
47:reliable medical references
10:
1847:
1697:alveolar–arterial gradient
1227:Kotz, John (August 2012).
1114:Principles of Biochemistry
716:
712:
194:Structure of oxyhemoglobin
1770:
1646:
1620:
1578:respiratory minute volume
1531:
1490:ventral respiratory group
1449:
1356:
1290:"Section 4/4ch5/s4ch5_18"
1164:Biochemistry Free For All
1149:Biochemistry Free For All
1071:Biochemistry Free For All
909:, SCN, which is excreted
765:heteroallosteric effector
534:
510:
489:
470:
180:of oxygen in the blood (P
147:oxygen dissociation curve
53:or relies too heavily on
1485:dorsal respiratory group
1379:obligate nasal breathing
1202:Schmidt-Nielsen (1997).
1016:
753:congestive heart failure
747:, chronic lung disease,
1687:pulmonary gas pressures
579:2,3-bisphosphoglycerate
452:2,3-bisphosphoglycerate
413:) falls 50 mmHg).
1816:Respiratory physiology
1441:mechanical ventilation
1350:Respiratory physiology
1177:Donna, Larson (2017).
1134:Respiratory Physiology
1132:Jacquez, John (1979).
965:
825:Hemoglobin binds with
811:
743:availability, such as
365:
298:
195:
1692:alveolar gas equation
1628:pulmonary circulation
963:
946:allosteric modulation
899:hexacyanoferrate(III)
812:
690:Allosteric regulation
621:
366:
296:
193:
1747:respiratory quotient
1602:body plethysmography
1521:Hering–Breuer reflex
1396:pulmonary surfactant
927:superoxide dismutase
781:
676:accumulation causes
566:Right shift: lower O
559:Left shift: higher O
312:
1590:Lung function tests
1424:hyperresponsiveness
1089:"Medical mnemonics"
805:
682:carbaminohemoglobin
618:temperature rises.
593:, face Right!" for
1821:Chemical pathology
1757:diffusion capacity
1752:arterial blood gas
1732:carbonic anhydrase
1466:pneumotaxic center
1006:Automated analyzer
966:
942:inositol phosphate
891:cytochrome oxidase
859:Methemoglobinaemia
807:
793:
361:
299:
196:
141:, also called the
1803:
1802:
1711:Oxygen saturation
1677:zones of the lung
1416:airway resistance
1288:Nosek, Thomas M.
1270:978-0-7817-6960-0
1188:978-1-4557-4214-1
879:cyanide poisoning
840:carboxyhemoglobin
796:
787:
761:hypophosphataemia
688:is considered an
553:
552:
356:
275:oxygen saturation
183:
172:
167:oxygen saturation
135:
134:
111:
16:(Redirected from
1838:
1612:nitrogen washout
1471:apneustic center
1386:respiratory rate
1343:
1336:
1329:
1320:
1319:
1301:
1296:. Archived from
1275:
1274:
1257:
1251:
1250:
1248:
1247:
1224:
1218:
1217:
1199:
1193:
1192:
1174:
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1159:
1153:
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1144:
1138:
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1129:
1118:
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1096:
1085:
1079:
1078:
1076:
1065:
1048:
1045:
1039:
1033:
1027:
973:adult hemoglobin
969:Fetal hemoglobin
956:Fetal hemoglobin
816:
814:
813:
808:
806:
804:
801:
794:
792:
785:
694:intracellular pH
636:
629:
460:Control factors
457:
370:
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279:partial pressure
219:prosthetic group
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178:partial pressure
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1790:oxygen toxicity
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1654:ventilation (V)
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1638:pulmonary shunt
1616:
1607:peak flow meter
1527:
1445:
1352:
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1313:
1284:
1279:
1278:
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1259:
1258:
1254:
1245:
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1241:
1225:
1221:
1214:
1200:
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1189:
1175:
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1160:
1156:
1145:
1141:
1130:
1121:
1110:
1103:
1094:
1092:
1087:
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1074:
1066:
1062:
1057:
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1043:
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1024:
1019:
1002:
958:
935:
933:Effects of ITPP
920:
866:oxidation state
856:
849:
837:
834:+ CO → HbCO + O
833:
827:carbon monoxide
823:
821:Carbon monoxide
802:
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725:red blood cells
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466:Shift of curve
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256:red blood cells
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55:primary sources
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1583:FEV1/FVC ratio
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1498:chemoreceptors
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1406:elastic recoil
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1302:
1300:on 2016-03-24.
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1282:External links
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1240:978-1133420071
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1212:
1194:
1187:
1169:
1154:
1139:
1119:
1101:
1080:
1059:
1058:
1056:
1053:
1050:
1049:
1021:
1020:
1018:
1015:
1014:
1013:
1008:
1001:
998:
957:
954:
934:
931:
918:
855:
852:
847:
835:
831:
822:
819:
800:
791:
773:
770:
740:
733:conjugate base
717:Main article:
714:
711:
706:
702:
697:
685:
673:
670:Carbon dioxide
666:
665:Carbon dioxide
663:
658:
646:
642:
623:
620:
598:
583:
582:
574:
571:
567:
564:
560:
551:
550:
547:
543:
542:
539:
536:
532:
531:
528:
524:
523:
520:
517:
513:
508:
507:
504:
500:
499:
496:
493:
487:
486:
483:
479:
478:
475:
472:
468:
467:
464:
461:
436:
433:
428:
424:
417:
410:
403:
399:
395:
390:
385:
372:
371:
360:
352:
349:
345:
341:
338:
334:
329:
326:
323:
320:
317:
290:
287:
268:carbon dioxide
226:carbon dioxide
200:
197:
184:
173:
163:oxygen tension
133:
132:
125:
123:
42:
40:
33:
26:
9:
6:
4:
3:
2:
1843:
1832:
1829:
1827:
1824:
1822:
1819:
1817:
1814:
1813:
1811:
1796:
1793:
1791:
1788:
1784:
1781:
1780:
1779:
1778:high altitude
1776:
1775:
1773:
1771:Insufficiency
1769:
1762:
1758:
1755:
1753:
1750:
1748:
1745:
1743:
1742:oxyhemoglobin
1740:
1737:
1733:
1730:
1727:
1724:
1722:
1719:
1717:
1714:
1712:
1708:
1705:
1703:
1700:
1698:
1695:
1693:
1690:
1688:
1685:
1683:
1680:
1678:
1675:
1671:
1668:
1666:
1663:
1662:
1660:
1657:
1655:
1652:
1651:
1649:
1645:
1639:
1636:
1634:
1631:
1629:
1626:
1625:
1623:
1619:
1613:
1610:
1608:
1605:
1603:
1600:
1598:
1595:
1593:
1591:
1588:
1587:
1584:
1581:
1579:
1576:
1574:
1571:
1570:
1567:
1564:
1562:
1559:
1557:
1554:
1552:
1549:
1547:
1544:
1542:
1539:
1538:
1536:
1534:
1530:
1522:
1519:
1518:
1517:
1514:
1510:
1507:
1505:
1502:
1501:
1500:
1499:
1495:
1491:
1488:
1486:
1483:
1482:
1481:
1480:
1476:
1472:
1469:
1467:
1464:
1463:
1462:
1461:
1457:
1456:
1454:
1452:
1448:
1442:
1439:
1435:
1432:
1430:
1427:
1425:
1422:
1421:
1419:
1417:
1414:
1412:
1411:hysteresivity
1409:
1407:
1404:
1402:
1399:
1397:
1394:
1392:
1389:
1387:
1384:
1380:
1377:
1375:
1372:
1370:
1367:
1366:
1365:
1362:
1361:
1359:
1355:
1351:
1344:
1339:
1337:
1332:
1330:
1325:
1324:
1321:
1315:
1308:
1306:
1303:
1299:
1295:
1291:
1286:
1285:
1272:
1266:
1262:
1256:
1242:
1236:
1232:
1231:
1223:
1215:
1209:
1205:
1198:
1190:
1184:
1180:
1173:
1165:
1158:
1150:
1143:
1135:
1128:
1126:
1124:
1115:
1108:
1106:
1090:
1084:
1073:
1072:
1064:
1060:
1046:
1040:
1034:
1026:
1022:
1012:
1009:
1007:
1004:
1003:
997:
994:
990:
984:
980:
976:
974:
970:
962:
953:
951:
947:
943:
939:
930:
928:
924:
916:
912:
908:
904:
900:
896:
892:
888:
884:
880:
876:
871:
867:
864:
860:
851:
845:
841:
828:
818:
798:
789:
769:
766:
762:
758:
754:
750:
746:
738:
734:
730:
726:
720:
710:
695:
691:
683:
679:
671:
662:
656:
652:
645:for a given P
639:
632:
619:
616:
612:
608:
604:
596:
592:
588:
580:
572:
565:
558:
557:
556:
548:
545:
544:
540:
537:
533:
529:
526:
525:
521:
518:
516:
509:
505:
502:
501:
497:
494:
492:
488:
484:
481:
480:
476:
473:
469:
465:
462:
459:
458:
455:
453:
448:
444:
441:
432:
421:
414:
407:
388:
379:
375:
358:
350:
347:
343:
339:
336:
332:
327:
321:
315:
308:
307:
306:
304:
295:
289:Sigmoid shape
286:
284:
280:
276:
271:
269:
265:
261:
260:carbonic acid
257:
253:
248:
246:
241:
239:
234:
229:
227:
222:
220:
217:
213:
209:
205:
192:
188:
179:
168:
164:
160:
156:
152:
148:
144:
140:
124:
120:
117:November 2021
109:
106:
102:
99:
95:
92:
88:
85:
81:
78: –
77:
73:
72:Find sources:
67:
63:
57:
56:
52:
48:
43:This article
41:
32:
31:
19:
1706:
1682:gas exchange
1647:Interactions
1572:calculations
1533:Lung volumes
1496:
1477:
1458:
1429:constriction
1391:respirometer
1298:the original
1293:
1260:
1255:
1244:. Retrieved
1229:
1222:
1203:
1197:
1178:
1172:
1163:
1157:
1148:
1142:
1133:
1113:
1093:. Retrieved
1091:. LifeHugger
1083:
1070:
1063:
1042:
1036:
1030:
1025:
985:
981:
977:
967:
936:
923:free radical
910:
887:amyl nitrite
857:
824:
775:
757:septic shock
722:
668:
641:binds less O
625:
614:
613:xercise and
610:
606:
602:
594:
590:
584:
554:
471:Temperature
449:
445:
442:
438:
422:
415:
408:
380:
376:
373:
300:
272:
249:
242:
230:
223:
202:
150:
146:
142:
138:
136:
114:
104:
97:
90:
83:
71:
51:verification
44:
1721:Bohr effect
1621:Circulation
1357:Respiration
1112:Lehninger.
1011:Bohr effect
907:thiocyanate
903:thiosulfate
895:vasodilator
772:Temperature
731:and is the
655:root effect
651:Bohr effect
264:capillaries
45:needs more
1826:Hematology
1810:Categories
1783:death zone
1702:hemoglobin
1597:spirometry
1556:dead space
1509:peripheral
1434:dilatation
1420:bronchial
1401:compliance
1374:exhalation
1369:inhalation
1246:2015-07-01
1213:0521570980
1095:2009-12-19
1055:References
915:superoxide
863:ferrous +2
729:glycolysis
204:Hemoglobin
199:Background
159:hemoglobin
87:newspapers
1659:Perfusion
885:(such as
870:ferric +3
790:−
745:hypoxemia
678:carbamino
605:cid, 2,3-
535:Acidity
348:−
1670:V/Q scan
1000:See also
989:placenta
587:mnemonic
570:affinity
563:affinity
266:, where
153:), is a
1795:hypoxia
1716:2,3-BPG
1504:central
1479:medulla
1451:Control
993:2,3-BPG
950:hypoxia
883:nitrite
875:cyanide
844:hypoxia
727:during
713:2,3-BPG
635:
628:
491:2,3-BPG
463:Change
389:. The P
303:sigmoid
243:In the
238:tissues
210:in the
101:scholar
66:removed
1831:Oxygen
1364:breath
1267:
1237:
1210:
1185:
1041:hospho
759:, and
751:, and
749:anemia
555:Note:
252:plasma
208:oxygen
176:) and
103:
96:
89:
82:
74:
1075:(PDF)
1017:Notes
591:CADET
245:lungs
212:blood
155:curve
108:JSTOR
94:books
1761:DLCO
1661:(Q)
1460:pons
1265:ISBN
1235:ISBN
1208:ISBN
1183:ISBN
684:. CO
609:PG,
216:heme
137:The
80:news
49:for
1566:PEF
1546:FRC
917:, O
911:via
830:HbO
735:of
589:, "
512:pCO
431:).
151:ODC
145:or
1812::
1561:CC
1551:Vt
1541:VC
1292:.
1122:^
1104:^
929:.
786:Hb
647:O2
622:pH
601:,
549:←
546:↓
541:→
538:↑
530:←
527:↓
522:→
519:↑
506:←
503:↓
498:→
495:↑
485:←
482:↓
477:→
474:↑
404:50
400:50
396:50
391:50
386:50
233:pH
221:.
169:(S
68:.
1763:)
1759:(
1738:)
1734:(
1728:)
1709:(
1342:e
1335:t
1328:v
1312:2
1273:.
1249:.
1216:.
1191:.
1098:.
1044:G
1038:P
1035:i
1032:D
919:2
848:2
836:2
832:2
799:2
795:O
741:2
707:2
703:2
698:2
686:2
674:2
659:2
643:2
638:H
631:H
615:T
611:E
607:D
603:A
599:2
597:O
595:C
581:.
575:2
568:2
561:2
514:2
429:2
425:2
418:2
411:2
394:P
384:P
359:.
351:t
344:e
340:+
337:1
333:1
328:=
325:)
322:t
319:(
316:S
185:2
182:O
174:2
171:O
149:(
119:)
115:(
105:·
98:·
91:·
84:·
58:.
20:)
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