Deoxygenation Of Erythrocytes Research Articles

Sudden sensorineural hearing loss in COVID-19 patient with hearing improvement

Introduction: Sudden Sensorineural Hearing Loss (SSNHL) is a newly revealed clinical manifestation in COVID-19 patients. This is because corona virus is thought to cause auditory neuropathy spectrum disorders, inflammation, hypoxia due to erythrocyte deoxygenation, ischemia due to vascular occlusion, and immunological reactions that induce cellular stress pathways in peripheral to central auditory organs. Case: A case of SSNHL in patient who were confirmed positive for PCR swab. A 66-year-old man with severe COVID-19, with hypertension and DM, had moderate right SNHL, left severe SNHL, when the PCR swab result was negative. Therapy received: methylcobalamin, gingkobiloba, HBOT, and the hearing was improved. Conclusion: SSNHL was obtained in COVID-19 patient.

Facile L-Glutamine delivery to erythrocytes via DOPC-DPPG mixed liposomes

Sickle cell disease (SCD) is a mortal erythrocyte-based disease which is hard to treat effectively. Development of a treatment method that can prevent deoxygenation of erythrocytes or reduce the oxidative stress of sickle erythrocytes is one of the important issues towards SCD. Among a wide variety of potential drug carriers, liposomes are advantageous and preferable with their easy preparation and biocompatibility. In this study, L-Glutamine (Gln) loaded liposomes were prepared with 1,2-Dioleoyl-sn-glycero-3-phosphocholine (DOPC) and 1,2-Dioleoyl-sn-glycero-3-phospho-rac-(1-glycerol) sodium salt (DPPG). Liposomes were characterized via zeta potential, size measurements, differential scanning calorimetry, Fourier Transform Infra-red Spectroscopy and they were visualized via transmission electron microscopy and scanning electron microscopy. Effect of the encapsulated amount of Gln was investigated by encapsulating Gln at three different concentrations (i.e0.20 mM, 40 mM and 60 mM). Drug encapsulation and release studies were implemented with high pressure liquid chromatography (HPLC). The encapsulation efficiency of Gln was determined to be the higher than the ones reported in the literature: 83.6%, 87.1% and 84.9% for 20 mM, 40 mM and 60 mM Gln, respectively. It was found that after 6 hours, liposomes loaded with 60 mM of Gln had released 45.7% of Gln. Optical microscopy images of the erythrocytes after 3 hours of incubation and haemolysis measurements proved that presence of liposomes did not cause any structural changes on the erythrocyte shape. Overall, it was concluded that L-Gln loaded PC/PG liposomes provide promising results in terms of developing a new drug delivery platform for SCD.

Preparation of L-Glutamine Loaded Liposomes for Drug Delivery to Erythrocytes

Sickle cell disease (SCD) is a mortal chronic disease caused by a point mutation in the ? chain gene in the hemoglobin A (HbA) molecule. Erythrocyte polymerization in SCD is mostly seen as a result of the decrease in the amount of ions and water in the cell, i.e. dehydration and deoxygenation of erythrocytes. Deoxygenated and dehydrated erythrocytes become susceptible to clustering, causing clogging of blood vessels which then leads to crisis. Therefore, development of a new treatment method that can effectively prevent deoxygenation of erythrocytes or reduce the oxidative stress of sickle erythrocytes is one of the important issues. The aim of this study is to obtain a new lipid-based drug delivery system that will further be used for decreasing the oxidative stress of sickle erythrocytes. For the purpose, in this study, L-Glutamine (L-Gln) loaded liposomal drug delivery system composed of L-?-Phosphatidylinositol (PI) is prepared. Also, effect of encapsulated amount of L-Gln in liposomes is investigated. Liposomes are prepared via thin-film rehydration method. Characterizations of liposomes are implemented with pH measurements, zeta potential and size measurements. Erythrocytes and liposomes are incubated at 37ºC for 1 and 3 hours. Interactions between the erythrocytes and liposomes are investigated via optical microscopy and hemolysis experiments. The size and zeta potential of unloaded PI liposomes are determined as 89.01 nm with a polydispersity index of 0.438 and -23.4 ± 1.5 mV, respectively. Sizes of L-Gln loaded liposomes are obtained as 126.7, 148.6 and 197.2 nm for 20 mM, 40 mM and 60 mM of L-Gln, respectively. From the optical microscopy images, it is determined that as incubation period of erythrocytes and liposomes are increased, more liposomes are interacted with erythrocytes. Also, as L-Gln amount is increased within the liposomes, it was observed that erythrocytes preserve their morphology. Overall, with this study, it can be concluded that L-Glutamine loaded liposomes can be used as a new drug delivery platform for erythrocytes. Moreover, the results of this study provide preliminary steps and promising results for design and development of a lipid-based drug carrier system to be used in the treatment of specific erythrocyte-based diseases such as sickle-cell disease.

Diffusion of glycophorin A in human erythrocytes

Several lines of evidence suggest that glycophorin A (GPA) interacts with band 3 in human erythrocyte membranes including: i) the existence of an epitope shared between band 3 and GPA in the Wright b blood group antigen, ii) the fact that antibodies to GPA inhibit the diffusion of band 3, iii) the observation that expression of GPA facilitates trafficking of band 3 from the endoplasmic reticulum to the plasma membrane, and iv) the observation that GPA is diminished in band 3 null erythrocytes. Surprisingly, there is also evidence that GPA does not interact with band 3, including data showing that: i) band 3 diffusion increases upon erythrocyte deoxygenation whereas GPA diffusion does not, ii) band 3 diffusion is greatly restricted in erythrocytes containing the Southeast Asian Ovalocytosis mutation whereas GPA diffusion is not, and iii) most anti-GPA or anti-band 3 antibodies do not co-immunoprecipitate both proteins. To try to resolve these apparently conflicting observations, we have selectively labeled band 3 and GPA with fluorescent quantum dots in intact erythrocytes and followed their diffusion by single particle tracking. We report here that band 3 and GPA display somewhat similar macroscopic and microscopic diffusion coefficients in unmodified cells, however perturbations of band 3 diffusion do not cause perturbations of GPA diffusion. Taken together the collective data to date suggest that while weak interactions between GPA and band 3 undoubtedly exist, GPA and band 3 must have separate interactions in the membrane that control their lateral mobility.

A Flow Cytometric Analysis of the Inhibition of Platelet Reactivity Due to Nitrite Reduction by Deoxygenated Erythrocytes

Nitric oxide (NO), a small gas molecule, has long been known to be a potent inhibitor of platelet function but the physiological and pathological implications of platelet inhibition by NO have not been well clarified. We recently showed that the addition of nitrite to platelet-rich plasma in the presence of erythrocytes could inhibit platelet aggregation and this inhibitory effect of nitrite + erythrocytes was enhanced by deoxygenation of erythrocytes as measured by P-selectin expression and cGMP production. In order to study the nitrite effect on platelets at different oxygen levels, we used the flow cytometric assays to detect platelet membrane surface markers upon activation. The P-selectin and activated gpIIb/IIIa expression on platelet membranes in response to ADP, collagen and thrombin stimulation was measured at various hematocrit and oxygen levels. Nitrite (0.1 to 1.0 μM) significantly decreased the percentage of these surface markers on the platelet membrane at the hematocrit values above 23% and oxygen levels lower than 49 mmHg. The inhibitory effect of nitrite was augmented by increasing hematocrit values and decreasing oxygen saturation. C-PTIO (an NO scavenger) prevented the platelet inhibition by nitrite + erythrocytes whereas the inhibitors of NO synthase and xanthine oxidoreductase had no effect. These results support the proposal that circulating nitrite decreases platelet reactivity in the presence of partially deoxygenated erythrocytes through its reduction to NO, which may also explain certain differences between arterial and venous thrombosis and support directly the role of deoxyhemoglobin in this process. We believe that our flow cytometric assays offer a possibility to identify the individual molecular process involved in these effects.

A FLOW–CYTOMETRIC ANALYSIS OF THE INHIBITION OF PLATELET REACTIVITY WITH NITRITE REDUCTION BY DEOXYGENATED ERYTHROCYTES

Nitric oxide (NO), a small gas molecule, has long been known to be a potent inhibitor of platelet function but the physiological and pathological implications of platelet inhibition by NO have not been well clarified. We recently showed that the addition of nitrite to platelet-rich plasma in the presence of erythrocytes could inhibit platelet aggregation and this inhibitory effect of nitrite + erythrocytes was enhanced by deoxygenation of erythrocytes as measured by P-selectin expression and cGMP production. In order to study the nitrite effect on platelets at different oxygen levels, we used the flow cytometric assays to detect platelet membrane surface markers upon activation. The P-selectin and activated gpIIb/IIIa expression on platelet membranes in response to ADP, collagen and thrombin stimulation was measured at various hematocrit and oxygen levels. Nitrite (0.1 to 1.0 mM) significantly decreased the percentage of these surface markers on the platelet membrane at the hematocrit values above 23% and oxygen levels lower than 49 mmHg. The inhibitory effect of nitrite was augmented by increasing hematocrit values and decreasing oxygen saturation. C-PTIO (an NO scavenger) prevented the platelet inhibition by nitrite + erythrocytes whereas the inhibitors of NO synthase and xanthine oxidoreductase had no effect. These results support the proposal that circulating nitrite decreases platelet reactivity in the presence of partially deoxygenated erythrocytes through its reduction to NO, which may also explain certain differences between arterial and venous thrombosis and support directly the role of deoxyhemoglobin in this process. We believe that our flow cytometric assays offer a possibility to identify the individual molecular process involved in these effects.

Nitrite Inhibits Platelet Reactivity in Presence of Deoxygenated Red Blood Cells As Measured by Flow Cytometry

AbstractAbstract 5146Nitric oxide (NO), a small gas molecule with multiple functions in the body, has been shown to have several precursors in body, the most abundant of which is nitrite. In the last decade several studies show that nitrite is reduced to NO by various enzymatic and non-enzymatic reductive processes, especially at low oxygenation conditions. These pathways are alternative mammalian sources of NO as compared to its enzymatic production by a family of nitric oxide synthase enzymes (NOS). NO has long been known to be a potent inhibitor of platelet function but the physiological and pathological implications of this has not been well clarified. We recently showed that addition of nitrite into plasma in the presence of red blood cells inhibits platelet aggregation and that this effect, as measured by cGMP production is enhanced by deoxygenation of erythrocytes. In order to study these effects more thoroughly on the molecular level, we have been developing flow-cytometric assays to study molecular processes on the platelet cell membrane known to correlate with platelet aggregation. We focused on P-selectin (CD62P) and activated GpIIb/IIIa (PAC-1) levels in platelets exposed to three activators, ADP, collagen and thrombin, in the presence of various concentrations of red blood cells and at variable levels of oxygen. We found that nitrite at physiological concentration (0. 1 to 1. 0 uM) significantly inhibited exposure of both of these surface markers on the outer membrane of platelets at levels of hematocrit above 23% and mean oxygen levels lower than 49 mmHg. The effect increased with increasing hematocrit and decreasing oxygen saturation into the hypoxic range. Addition of an NO scavenger prevented nitrite-related platelet inhibition, but addition of an inhibitor of NOS or of xanthine oxidoreductase had no effect. These results indicate that physiological levels of nitrite ions in the blood can modulate platelet reactivity in the presence of partially deoxygenated erythrocytes by the reduction to NO and that this process can modulate platelet activation and aggregation levels and confirm and extend our previous report (Srihirun et al, PLoS One 7, e30380, 2012), done primarily using aggregation assays. Our flow cytometry assays not only allows a more detailed and systematic study of the kinetics and equilibrium aspects of the aggregation process, but also offers a possibility to identify the individual molecular processes involved in these effects. The results may also explain certain differences between arterial and venous thrombosis. Disclosures:Schechter:NIH: Employment, co-inventor of NIH patent on use of nitrite in disease, co-inventor of NIH patent on use of nitrite in disease Patents & Royalties.

Impaired Skeletal Muscle Blood Flow Control With Advancing Age in Humans

Rationale: Skeletal muscle blood flow is coupled with the oxygenation state of hemoglobin in young adults, whereby the erythrocyte functions as an oxygen sensor and releases ATP during deoxygenation to evoke vasodilation. Whether this function is impaired in humans of advanced age is unknown. Objective: To test the hypothesis that older adults demonstrate impaired muscle blood flow and lower intravascular ATP during conditions of erythrocyte deoxygenation. Methods and Results: We showed impaired forearm blood flow responses during 2 conditions of erythrocyte deoxygenation (systemic hypoxia and graded handgrip exercise) with age, which was caused by reduced local vasodilation. In young adults, both hypoxia and exercise significantly increased venous [ATP] and ATP effluent (forearm blood flow×[ATP]) draining the skeletal muscle. In contrast, hypoxia and exercise did not increase venous [ATP] in older adults, and both venous [ATP] and ATP effluent were substantially reduced compared with young people despite similar levels of deoxygenation. Next, we demonstrated that this could not be explained by augmented extracellular ATP hydrolysis in whole blood with age. Finally, we found that deoxygenation-mediated ATP release from isolated erythrocytes was essentially nonexistent in older adults. Conclusions: Skeletal muscle blood flow during conditions of erythrocyte deoxygenation was markedly reduced in aging humans, and reductions in plasma ATP and erythrocyte-mediated ATP release may be a novel mechanism underlying impaired vasodilation and oxygen delivery during hypoxemia with advancing age. Because aging is associated with elevated risk for ischemic cardiovascular disease and exercise intolerance, interventions that target erythrocyte-mediated ATP release may offer therapeutic potential.

SNO-hemoglobin is not essential for red blood cell–dependent hypoxic vasodilation

The coupling of hemoglobin sensing of physiological oxygen gradients to stimulation of nitric oxide (NO) bioactivity is an established principle of hypoxic blood flow. One mechanism proposed to explain this oxygen-sensing-NO bioactivity linkage postulates an essential role for the conserved Cys93 residue of the hemoglobin beta-chain (betaCys93) and, specifically, for S-nitrosation of betaCys93 to form S-nitrosohemoglobin (SNO-Hb). The SNO-Hb hypothesis, which conceptually links hemoglobin and NO biology, has been debated intensely in recent years. This debate has precluded a consensus on physiological mechanisms and on assessment of the potential role of SNO-Hb in pathology. Here we describe new mouse models that exclusively express either human wild-type hemoglobin or human hemoglobin in which the betaCys93 residue is replaced with alanine to assess the role of SNO-Hb in red blood cell-mediated hypoxic vasodilation. Substitution of this residue, precluding hemoglobin S-nitrosation, did not change total red blood cell S-nitrosothiol abundance but did shift S-nitrosothiol distribution to lower molecular weight species, consistent with the loss of SNO-Hb. Loss of betaCys93 resulted in no deficits in systemic or pulmonary hemodynamics under basal conditions and, notably, did not affect isolated red blood cell-dependent hypoxic vasodilation. These results demonstrate that SNO-Hb is not essential for the physiologic coupling of erythrocyte deoxygenation with increased NO bioactivity in vivo.

Stimulation of Na +/Mg 2+ antiport in rat erythrocytes by intracellular Cl −

Mg 2+ efflux from rat erythrocytes was measured in NaCl, NaNO 3, NaSCN and Na gluconate medium. Substitution of extracellular and intracellular Cl − with the permeant anions NO 3 − and SCN − reduced Mg 2+ efflux via Na +/Mg 2+ antiport. After substitution of extracellular Cl − with the non-permeant anion gluconate, Mg 2+ efflux was not significantly reduced. In Na gluconate medium, an influence of the changed membrane potential and intracellular pH on Mg 2+ efflux could be excluded. The results indicate the existence of Cl −-independent Na +/Mg 2+ antiport and of Na +/Mg 2+ antiport stimulated by intracellular Cl −. Intracellular Cl −, as determined by means of 36Cl −, was found to stimulate Na +/Mg 2+ antiport through a cooperative effect according to a sigmoidal kinetics. The Hill coefficient for intracellular Cl − amounted to 1.4–1.8, indicating that two intracellular Cl − may be simultaneously active. With respect to specificity, Cl − was most effective, followed by Br −, J −, and F −. Stimulation of Na +/Mg 2+ antiport by intracellular Cl − together with intracellular Mg 2+ may play a role during deoxygenation of erythrocytes and in essential hypertension.

The ventilatory response to hypoxia

We do not challenge the 'classic' theory of peripheral-chemoreceptor-mediated HVR. However, this offers no insight into the mediators of the time-domain components of HVR, such as ventilatory short-term potentiation (VSTP)1. VSTP is critical to respiratory-system stability2 and is unrelated to the activity of the peripheral chemoreceptor3,4, so other factors may have a role in HVR5,6. One such factor involves SNO signalling in brainstem neurons. SNOs could be formed by neuronal nitric oxide synthase (NOS, activated by afferents from peripheral chemoreceptors) and by erythrocyte deoxygenation. Indeed, erythrocyte deoxygenation could be signalled to peripheral chemoreceptors through SNO formation.

Imaging of oxygen saturation and distribution of erythrocytes in microvessels.

To construct images of oxygen saturation and the distribution of erythrocytes in a network of microvessels. The image of a small group of microvessels under an inverted microscope was incorporated into an image processor through a video camera and was digitized. Based on the information obtained through six visible interference filters of different wavelengths, oxygen saturation and the amount of erythrocytes in microvessels were calculated with a computer. The system was applied to a microvascular bed of isolated rabbit mesentery perfused with a suspension of human erythrocytes. In a steady flow, with lowering of tissue oxygen tension by superfusion with nitrogen-bubbled isotonic saline containing 20 mmol/L sodium dithionite, the decrease of oxygen saturation of erythrocytes from arterioles to venules was imaged. Simultaneously, the distribution of erythrocytes in the microvessels was imaged and the marginal cell-free layer was profiled under high magnification. No significant alteration of the erythrocyte distribution on the deoxygenation of erythrocytes was observed. The exposure of erythrocytes to acidic pH and the decrease of the flow velocity of erythrocytes increased the release of oxygen from the erythrocytes in microvessels. The present method will be useful for the comprehensive analysis of oxygen transfer in the microvascular network, on the basis of both changes of the oxygen saturation and the flow behavior of erythrocytes.

Activation of the alternative complement pathway by exposure of phosphatidylethanolamine and phosphatidylserine on erythrocytes from sickle cell disease patients.

Deoxygenation of erythrocytes from sickle cell anemia (SCA) patients alters membrane phospholipid distribution with increased exposure of phosphatidylethanolamine (PE) and phosphatidylserine (PS) on the outer leaflet. This study investigated whether altered membrane phospholipid exposure on sickle erythrocytes results in complement activation. In vitro deoxygenation of sickle but not normal erythrocytes resulted in complement activation measured by C3 binding. Additional evidence indicated that this activation was the result of the alterations in membrane phospholipids. First, complement was activated by normal erythrocytes after incubation with sodium tetrathionate, which produces similar phospholipid changes. Second, antibody was not required for complement activation by sickle or tetrathionate-treated erythrocytes. Third, the membrane regulatory proteins, decay-accelerating factor (CD55) and the C3b/C4b receptor (CD35), were normal on sickle and tetrathionate-treated erythrocytes. Finally, insertion of PE or PS into normal erythrocytes induced alternative pathway activation. SCA patients in crisis exhibited increased plasma factor Bb levels compared with baseline, and erythrocytes isolated from hospitalized SCA patients had increased levels of bound C3, indicating that alternative pathway activation occurs in vivo. Activation of complement may be a contributing factor in sickle crisis episodes, shortening the life span of erythrocytes and decreasing host defense against infections.

Kinetics of oxygenation and deoxygenation of erythrocytes containing hemoglobin S

The rates of oxygenation and deoxygenation of erythrocytes from normal individuals and patients with sickle cell anemia have been measured at physiologic pH and temperature. The oxygenation reaction velocity constant for the cells from the patients was half that for cells from normal controls (44.5±14.8 mM −1 sec −1 as compared to 89.4±23.1 mM −1 sec −1). However the deoxygenation velocity constant for cells from patients was almost twice that for cells from the normal controls (20.8±2.4 sec −1 as compared to 11.0±1.6 sec −1). These differences in kinetic constants apparently result from alterations in the internal cellular environment rather than from the differences in structure of hemoglobin A and S. The factors responsible for the observed changes are not apparent. The decreased rate of oxygen uptake by hemoglobin S cells may possibly produce an end-capillary oxygen difference between blood and alveolar gas in areas of the lung with low ratios of diffusing capacity to blood flow.

Effect of 2,3-diphosphoglycerate and H+ on the raction of O 2 and hemoglobin.

ARTICLESEffect of 2,3-diphosphoglycerate and H+ on the raction of O 2 and hemoglobinC Bauer, RA Klocke, D Kamp, and RE ForsterC Bauer, RA Klocke, D Kamp, and RE ForsterPublished Online:01 Apr 1973https://doi.org/10.1152/ajplegacy.1973.224.4.838MoreSectionsPDF (3 MB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInWeChat Previous Back to Top Next Download PDF FiguresReferencesRelatedInformation Cited ByO2 permeability of lipid bilayers is low, but increases with membrane cholesterol25 October 2021 | Cellular and Molecular Life Sciences, Vol. 78, No. 23The rate of the deoxygenation reaction limits myoglobin- and hemoglobin-facilitated O2 diffusion in cellsVolker Endeward1 May 2012 | Journal of Applied Physiology, Vol. 112, No. 9Erratum to: Blood HbO2 and HbCO2 Dissociation Curves at Varied O2, CO2, pH, 2,3-DPG and Temperature Levels17 February 2010 | Annals of Biomedical Engineering, Vol. 38, No. 4The unpretentious role of 2,3-diphosphoglycerate in critical illness*Critical Care Medicine, Vol. 33, No. 10Blood HbO2 and HbCO2 Dissociation Curves at Varied O2, CO2, pH, 2,3-DPG and Temperature LevelsAnnals of Biomedical Engineering, Vol. 32, No. 12Reaction rates of oxygen with hemoglobin measured by non-equilibrium facilitated oxygen diffusion through hemoglobin solutionsBiochimica et Biophysica Acta (BBA) - General Subjects, Vol. 1525, No. 1-2Kinetics of Oxygen and Carbon Dioxide ExchangeDiffusion of Gases Across the Alveolar Membrane1 January 2011Blood Oxygen Transport1 January 2011Oxygen transfer conductance of human red blood cells at varied pH and temperatureRespiration Physiology, Vol. 67, No. 2Effects of Temperature on Oxygen Transfer Conductance of Human Red Blood CellsBlood-gas equilibria, kinetics and transportChemical Engineering Science, Vol. 42, No. 2Blood Gas Transport and 2,3-DPGKinetics of O2 uptake and release by red cells in stopped-flow apparatus: Effects of unstirred layerRespiration Physiology, Vol. 59, No. 1The reaction kinetics of four sheep haemoglobins with identical α-chainsRespiration Physiology, Vol. 53, No. 1Identification of residues contributing to the Bohr effect of human haemoglobinJournal of Molecular Biology, Vol. 138, No. 3Kinetics of Pulmonary Gas ExchangeThe pH Dependence of the Binding of d-Glycerate 2,3-Bisphosphate to Deoxyhemoglobin and Oxyhemoglobin. Determination of the Number of Binding Sites in OxyhemoglobinEuropean Journal of Biochemistry, Vol. 100, No. 2What is the Clinical Importance of Alterations of the Hemoglobin Oxygen Affinity in Preserved Blood - Especially as Produced by Variations of Red Cell 2, 3 DPG Content?Vox Sanguinis, Vol. 34, No. 2The Theoretical Effect of DPG Upon Oxygen Diffusion in Erythrocytes16 April 2012The oxyhemoglobin dissociation curve in health and diseaseThe American Journal of Medicine, Vol. 57, No. 3Kinetics of oxygenation and deoxygenation of erythrocytes containing hemoglobin SRespiration Physiology, Vol. 21, No. 1Influence of altitude training on muscle metabolism and performance in man.British Journal of Sports Medicine, Vol. 8, No. 1The oxygen affinity of axolotl blood and haemoglobin before and after metamorphosisRespiration Physiology, Vol. 18, No. 1 More from this issue > Volume 224Issue 4April 1973Pages 838-847 Copyright & PermissionsCopyright © 1973 by American Physiological Societyhttps://doi.org/10.1152/ajplegacy.1973.224.4.838PubMed4698800History Published online 1 April 1973 Published in print 1 April 1973 Metrics

Effect of anemia, species, and temperature on CO kinetics with red blood cells.

ArticleEffect of anemia, species, and temperature on CO kinetics with red blood cells.W H Lawson JrW H Lawson JrPublished Online:01 Sep 1971https://doi.org/10.1152/jappl.1971.31.3.447MoreSectionsPDF (3 MB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInWeChat Previous Back to Top Next Download PDF FiguresReferencesRelatedInformation Cited ByHigh-altitude exposure of three weeks duration increases lung diffusing capacity in humansPiergiuseppe Agostoni, Erik R. Swenson, Maurizio Bussotti, Miriam Revera, Paolo Meriggi, Andrea Faini, Carolina Lombardi, Grzegorz Bilo, Andrea Giuliano, Daniele Bonacina, Pietro A. Modesti, Giuseppe Mancia, and Gianfranco Paration behalf of the HIGHCARE Investigators1 June 2011 | Journal of Applied Physiology, Vol. 110, No. 6Rate of uptake of CO by hemoglobin in pig erythrocytes as a function of PO2Francis C. A. M. Te Nijenhuis, Lydia Lin, Gerko H. Moens, Adrian Versprille, and Robert E. Forster1 October 1996 | Journal of Applied Physiology, Vol. 81, No. 4Diffusion of Gases Across the Alveolar Membrane1 January 2011Alveolar-arterial equilibration in the lung of sheepRespiration Physiology, Vol. 55, No. 2Simultaneous O2 and CO diffusing capacity estimates from assumed lognormal V̇A, Q̇ and DL distributionsRespiration Physiology, Vol. 52, No. 1Pulmonary diffusing capacity in reptiles (Relations to temperature and O2-uptake)Journal of Comparative Physiology ? B, Vol. 142, No. 4Kinetics of Pulmonary Gas ExchangeTotal Body Haemoglobin Estimated with the Alveolar CO Method as Compared with a 51 Cr Technique18 January 2010 | Upsala Journal of Medical Sciences, Vol. 83, No. 1The biological effects of carbon monoxide on the pregnant woman, fetus, and newborn infantAmerican Journal of Obstetrics and Gynecology, Vol. 129, No. 1Kinetics of oxygenation and deoxygenation of erythrocytes containing hemoglobin SRespiration Physiology, Vol. 21, No. 1Influence of intracellular convection on the oxygen release by human erythrocytesPfl�gers Archiv European Journal of Physiology, Vol. 335, No. 1 More from this issue > Volume 31Issue 3September 1971Pages 447-57 https://doi.org/10.1152/jappl.1971.31.3.447PubMed5111864History Published online 1 September 1971 Published in print 1 September 1971 Metrics

Oxygen tension gradients in peripheral capillary blood.

ArticleOxygen tension gradients in peripheral capillary blood.W H Lawson Jr, and R E ForsterW H Lawson Jr, and R E ForsterPublished Online:01 May 1967https://doi.org/10.1152/jappl.1967.22.5.970MoreSectionsPDF (782 KB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInWeChat Previous Back to Top Next Download PDF FiguresReferencesRelatedInformationCited ByDietary Chlorophyll Metabolites Catalyze the Photoreduction of Plasma Ubiquinone26 September 2012 | Photochemistry and Photobiology, Vol. 89, No. 2Erythrocyte-associated transients in capillary Po2: an isovolemic hemodilution study in the rat spinotrapezius muscleMatthew C. Barker, Aleksander S. Golub, and Roland N. Pittman1 May 2007 | American Journal of Physiology-Heart and Circulatory Physiology, Vol. 292, No. 5A Multiparametric Assessment of Oxygen Efflux from the Brain22 June 2005 | Journal of Cerebral Blood Flow & Metabolism, Vol. 26, No. 1Erythrocyte-associated transients in Po2 revealed in capillaries of rat mesenteryAleksander S. Golub, and Roland N. Pittman1 June 2005 | American Journal of Physiology-Heart and Circulatory Physiology, Vol. 288, No. 6Dependence of Oxygen Delivery on Blood Flow in Rat Brain: A 7 Tesla Nuclear Magnetic Resonance Study31 August 2016 | Journal of Cerebral Blood Flow & Metabolism, Vol. 20, No. 3A model for the regulation of cerebral oxygen deliveryFahmeed Hyder, Robert G. Shulman, and Douglas L. Rothman1 August 1998 | Journal of Applied Physiology, Vol. 85, No. 2Transfer of Gas by Diffusion and Chemical Reaction in Pulmonary CapillariesDiffusion of Gases Across the Alveolar Membrane1 January 2011Theoretical analysis of oxygen transport during hypothermiaJournal of Clinical Monitoring, Vol. 2, No. 1The rate of oxygen release and its effect on capillary O2 tension: A mathematical analysisRespiration Physiology, Vol. 63, No. 1Oxygen gradients between red blood cells in the microcirculationMicrovascular Research, Vol. 22, No. 3Kinetics of Pulmonary Gas ExchangeWhat is the Clinical Importance of Alterations of the Hemoglobin Oxygen Affinity in Preserved Blood - Especially as Produced by Variations of Red Cell 2, 3 DPG Content?Vox Sanguinis, Vol. 34, No. 2The Effect of Deoxygenation Rate of the Erythrocyte on Oxygen Transport to the Cardiac Muscle16 April 2012The Theoretical Effect of DPG Upon Oxygen Diffusion in Erythrocytes16 April 2012Kinetics of oxygenation and deoxygenation of erythrocytes containing hemoglobin SRespiration Physiology, Vol. 21, No. 1 More from this issue > Volume 22Issue 5May 1967Pages 970-3 https://doi.org/10.1152/jappl.1967.22.5.970PubMed6025755History Published online 1 May 1967 Published in print 1 May 1967 Metrics