Biochimica Et Biophysica Acta - Proteins And Proteomics, Sep 1, 2013
Recent years have witnessed a new round of research on one of the most studied proteins - myoglob... more Recent years have witnessed a new round of research on one of the most studied proteins - myoglobin (Mb), the oxygen (O2) carrier of skeletal and heart muscle. Two major discoveries have stimulated research in this field: 1) that Mb has additional protecting functions, such as the regulation of in vivo levels of the signaling molecule nitric oxide (NO) by scavenging and generating NO during normoxia and hypoxia, respectively; and 2) that Mb in vertebrates (particularly fish) is expressed as tissue-specific isoforms in other tissues than heart and skeletal muscle, such as vessel endothelium, liver and brain, as found in cyprinid fish. Furthermore, Mb has also been found to protect against oxidative stress after hypoxia and reoxygenation and to undergo allosteric, O2-linked S-nitrosation, as in rainbow trout. Overall, the emerging evidence, particularly from fish species, indicates that Mb fulfills a broader array of physiological functions in a wider range of different tissues than hitherto appreciated. This new knowledge helps to better understand how variations in Mb structure and function may correlate with differences in animals' lifestyles and hypoxia-tolerance. This review integrates old and new results on Mb expression patterns and functional properties amongst vertebrates and discusses how these may relate to adaptive variations in different species. This article is part of a special issue entitled: Oxygen Binding and Sensing Proteins.
Comparative biochemistry and physiology. B. Comparative biochemistry, 1976
1. 1. Haemoglobin from the coelomic cells of Glycera gigantea was studied with regard to molecula... more 1. 1. Haemoglobin from the coelomic cells of Glycera gigantea was studied with regard to molecular weight, subunit composition, heterogeneity on the basis of isoelectric point and oxygen equilibrium of the major components. 2. 2. In gel filtration chromatography the haemoglobin resolves into a main component (HbH) and a minor component of smaller molecules (HbL), which appear to be composed of protein chain subunits of the same size, but have sedimentation values, S20,w, of 4·4 and 1·6 indicative respectively, of tetramers and monomers. 3. 3. The haemoglobin is highly heterogeneous on the basis of isoelectric point. Six fractions studied funtionally show considerable differentiation in oxygen affinities. 4. 4. The data are discussed comparatively with particular reference to the coelomic haemoglobin of G. dibranchiata and vascular haemoglobin of Arenicola marina.
The oxygen-binding characteristics and the multiplicity of the stripped hemoglobiin from active l... more The oxygen-binding characteristics and the multiplicity of the stripped hemoglobiin from active lungfish Protopterus amphibius, are the same as in specimens that have been estivating for about 30 months, showing that alteration in the hemoglobin molecules is not involved in the earlier reported increase in oxygen affinity of whole blood during estivation (Johansen et al., '76). At pH 7.0 and 26 degrees C the hemolysates show a high oxygen affinity (P50 = 3.1 Torr), a Bohr factor (delta log P50/delta pH) of - 0.33, and a cooperativity coefficient (n) of 1.7. Between 15 and 26 degrees C, the apparent heat of oxygenation (delta H) is - 8.6 Kcal-mole-1 at pH 7.0, corresponding with data for other fish. A low sensitivity of oxygen affinity to urea appears to be adaptive to the high urea concentrations in estivating lungfish. The salt sensitivity is, however, similar to human hemoglobin. The hemoglobin consists of two major (electrophoretically anodal) components, which differ slightly in oxygen affinity but are both sensitive to pH and nucleoside triphosphates (NTP). Guanosine triphosphate (GTP), the major erythrocytic organic phosphate, however, depresses the oxygen affinity of the composite and separated hemoglobins more effectively than ATP suggesting that GTP is the primary modulator of oxygen affinity. Comparative measurements reveal only one major hemoglobin component in P. annectens which has a markedly lower oxygen affinity and phosphate sensitivity than P. amphibius hemoglobins and thus seems less pliable to phosphate-mediated variation in oxygen affinity. The data are discussed in relation to the hemoglobin systems of other fish.
Korean female unassisted divers (cachido ama) breath-hold dive > 100 times to depths of 3-... more Korean female unassisted divers (cachido ama) breath-hold dive > 100 times to depths of 3-7 m during a work day. We sought to determine the extent of arterial hypoxemia during normal working dives and reasonable time limits for breath-hold diving by measuring radial artery blood gas tensions and pH in five cachido ama who dove to a fixed depth of 4-5 m and then continued to breath hold for various times after their return to the surface. Eighty-two blood samples were withdrawn from indwelling radial artery catheters during 37 ocean dives. We measured compression hyperoxia [arterial PO2 = 141 +/- 24 (SD) Torr] and hypercapnia (arterial PCO2 = 46.6 +/- 2.4 Torr) at depth. Mean arterial PO2 near the end of breath-hold dives lasting 32-95 s (62 +/- 14 s) was decreased (62.6 +/- 13.5 Torr). Mean arterial PCO2 reached 49.9 +/- 5.4 Torr. Complete return of these values to their baseline did not occur until 15-20 s after breathing was resumed. In dives of usual working duration (< 30 s), blood gas tensions remained within normal ranges. Detailed analysis of hemoglobin components and intrinsic oxygenation properties revealed no evidence for adaptive changes that could increase the tolerance of the ama to hypoxic or hypothermic conditions associated with repetitive diving.
Oxygen equilibria of whole blood and hemoglobins from adult and fetal Weddell seals are reported.... more Oxygen equilibria of whole blood and hemoglobins from adult and fetal Weddell seals are reported. The maternal blood shows a lower O2 affinity than the fetal blood (halfsaturation O2 tension P50 = 26.9 +/- 1.18 and 21.4 +/- 1.25 Torr, respectively, at 37 degrees C and pH 7.4), and a greater Bohr effect (delta log P50/delta pH = -0.49 and -0.31, respectively, at pH 7.4-6.8), correlated with higher red cell 2,3-diphosphoglycerate (2,3-diphosphoglycerate (2,3-DPG) concentrations (6.45 +/- 0.81 mmol.1-1, compared to 2.65 +/- 0-42 mmol.1-1 in the fetus). Both the maternal and fetal erythrocytes contain two major and two minor hemoglobin components occurring in the same ratio and the 2,3-DPG-free whole hemolysates, as well as the isolated major components from each stage, show the same oxygenation properties, ascribing the whole-blood differences to the higher adult DPG levels. A 2,3-DPG effect also appears to account for the disparity in the Bohr effects, which will favor unloading of O2 from the maternal circulation during diving as maternal and fetal blood pH decrease in parallel.
Biochimica Et Biophysica Acta - Proteins And Proteomics, Sep 1, 2013
Recent years have witnessed a new round of research on one of the most studied proteins - myoglob... more Recent years have witnessed a new round of research on one of the most studied proteins - myoglobin (Mb), the oxygen (O2) carrier of skeletal and heart muscle. Two major discoveries have stimulated research in this field: 1) that Mb has additional protecting functions, such as the regulation of in vivo levels of the signaling molecule nitric oxide (NO) by scavenging and generating NO during normoxia and hypoxia, respectively; and 2) that Mb in vertebrates (particularly fish) is expressed as tissue-specific isoforms in other tissues than heart and skeletal muscle, such as vessel endothelium, liver and brain, as found in cyprinid fish. Furthermore, Mb has also been found to protect against oxidative stress after hypoxia and reoxygenation and to undergo allosteric, O2-linked S-nitrosation, as in rainbow trout. Overall, the emerging evidence, particularly from fish species, indicates that Mb fulfills a broader array of physiological functions in a wider range of different tissues than hitherto appreciated. This new knowledge helps to better understand how variations in Mb structure and function may correlate with differences in animals' lifestyles and hypoxia-tolerance. This review integrates old and new results on Mb expression patterns and functional properties amongst vertebrates and discusses how these may relate to adaptive variations in different species. This article is part of a special issue entitled: Oxygen Binding and Sensing Proteins.
Comparative biochemistry and physiology. B. Comparative biochemistry, 1976
1. 1. Haemoglobin from the coelomic cells of Glycera gigantea was studied with regard to molecula... more 1. 1. Haemoglobin from the coelomic cells of Glycera gigantea was studied with regard to molecular weight, subunit composition, heterogeneity on the basis of isoelectric point and oxygen equilibrium of the major components. 2. 2. In gel filtration chromatography the haemoglobin resolves into a main component (HbH) and a minor component of smaller molecules (HbL), which appear to be composed of protein chain subunits of the same size, but have sedimentation values, S20,w, of 4·4 and 1·6 indicative respectively, of tetramers and monomers. 3. 3. The haemoglobin is highly heterogeneous on the basis of isoelectric point. Six fractions studied funtionally show considerable differentiation in oxygen affinities. 4. 4. The data are discussed comparatively with particular reference to the coelomic haemoglobin of G. dibranchiata and vascular haemoglobin of Arenicola marina.
The oxygen-binding characteristics and the multiplicity of the stripped hemoglobiin from active l... more The oxygen-binding characteristics and the multiplicity of the stripped hemoglobiin from active lungfish Protopterus amphibius, are the same as in specimens that have been estivating for about 30 months, showing that alteration in the hemoglobin molecules is not involved in the earlier reported increase in oxygen affinity of whole blood during estivation (Johansen et al., '76). At pH 7.0 and 26 degrees C the hemolysates show a high oxygen affinity (P50 = 3.1 Torr), a Bohr factor (delta log P50/delta pH) of - 0.33, and a cooperativity coefficient (n) of 1.7. Between 15 and 26 degrees C, the apparent heat of oxygenation (delta H) is - 8.6 Kcal-mole-1 at pH 7.0, corresponding with data for other fish. A low sensitivity of oxygen affinity to urea appears to be adaptive to the high urea concentrations in estivating lungfish. The salt sensitivity is, however, similar to human hemoglobin. The hemoglobin consists of two major (electrophoretically anodal) components, which differ slightly in oxygen affinity but are both sensitive to pH and nucleoside triphosphates (NTP). Guanosine triphosphate (GTP), the major erythrocytic organic phosphate, however, depresses the oxygen affinity of the composite and separated hemoglobins more effectively than ATP suggesting that GTP is the primary modulator of oxygen affinity. Comparative measurements reveal only one major hemoglobin component in P. annectens which has a markedly lower oxygen affinity and phosphate sensitivity than P. amphibius hemoglobins and thus seems less pliable to phosphate-mediated variation in oxygen affinity. The data are discussed in relation to the hemoglobin systems of other fish.
Korean female unassisted divers (cachido ama) breath-hold dive > 100 times to depths of 3-... more Korean female unassisted divers (cachido ama) breath-hold dive > 100 times to depths of 3-7 m during a work day. We sought to determine the extent of arterial hypoxemia during normal working dives and reasonable time limits for breath-hold diving by measuring radial artery blood gas tensions and pH in five cachido ama who dove to a fixed depth of 4-5 m and then continued to breath hold for various times after their return to the surface. Eighty-two blood samples were withdrawn from indwelling radial artery catheters during 37 ocean dives. We measured compression hyperoxia [arterial PO2 = 141 +/- 24 (SD) Torr] and hypercapnia (arterial PCO2 = 46.6 +/- 2.4 Torr) at depth. Mean arterial PO2 near the end of breath-hold dives lasting 32-95 s (62 +/- 14 s) was decreased (62.6 +/- 13.5 Torr). Mean arterial PCO2 reached 49.9 +/- 5.4 Torr. Complete return of these values to their baseline did not occur until 15-20 s after breathing was resumed. In dives of usual working duration (< 30 s), blood gas tensions remained within normal ranges. Detailed analysis of hemoglobin components and intrinsic oxygenation properties revealed no evidence for adaptive changes that could increase the tolerance of the ama to hypoxic or hypothermic conditions associated with repetitive diving.
Oxygen equilibria of whole blood and hemoglobins from adult and fetal Weddell seals are reported.... more Oxygen equilibria of whole blood and hemoglobins from adult and fetal Weddell seals are reported. The maternal blood shows a lower O2 affinity than the fetal blood (halfsaturation O2 tension P50 = 26.9 +/- 1.18 and 21.4 +/- 1.25 Torr, respectively, at 37 degrees C and pH 7.4), and a greater Bohr effect (delta log P50/delta pH = -0.49 and -0.31, respectively, at pH 7.4-6.8), correlated with higher red cell 2,3-diphosphoglycerate (2,3-diphosphoglycerate (2,3-DPG) concentrations (6.45 +/- 0.81 mmol.1-1, compared to 2.65 +/- 0-42 mmol.1-1 in the fetus). Both the maternal and fetal erythrocytes contain two major and two minor hemoglobin components occurring in the same ratio and the 2,3-DPG-free whole hemolysates, as well as the isolated major components from each stage, show the same oxygenation properties, ascribing the whole-blood differences to the higher adult DPG levels. A 2,3-DPG effect also appears to account for the disparity in the Bohr effects, which will favor unloading of O2 from the maternal circulation during diving as maternal and fetal blood pH decrease in parallel.
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