ArticleAmerican journal of physiology. Regulatory, integrative and comparative physiology2015
Oxygenation properties and isoform diversity of snake hemoglobins.
Article in American journal of physiology. Regulatory, integrative and comparative physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 31 citations in OpenAlex.
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- New insights into the allosteric effects of CO2 and bicarbonate on crocodilian hemoglobin.The Journal of experimental biology · 2021Article
- Effect of NH2-terminal acetylation on the oxygenation properties of vertebrate haemoglobin.The Biochemical journal · 2020Article
- Biochemical pedomorphosis and genetic assimilation in the hypoxia adaptation of Tibetan antelope.Science advances · 2020Article
- Structure and function of crocodilian hemoglobins and allosteric regulation by chloride, ATP, and COAmerican journal of physiology. Regulatory, integrative and comparative physiology · 2020Article
- Oxygenation properties of hemoglobin and the evolutionary origins of isoform multiplicity in an amphibious air-breathing fish, the blue-spotted mudskipper (The Journal of experimental biology · 2020Article
- The role of mutation bias in adaptive molecular evolution: insights from convergent changes in protein function.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019Article
- Allosteric mechanisms underlying the adaptive increase in hemoglobin-oxygen affinity of the bar-headed goose.The Journal of experimental biology · 2018Article
- Divergent and parallel routes of biochemical adaptation in high-altitude passerine birds from the Qinghai-Tibet Plateau.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Gene Turnover and Diversification of the α- and β-Globin Gene Families in Sauropsid Vertebrates.Genome biology and evolution · 2018Article
- Stability-Mediated Epistasis Restricts Accessible Mutational Pathways in the Functional Evolution of Avian Hemoglobin.Molecular biology and evolution · 2017Article
- Hemoglobin-oxygen affinity in high-altitude vertebrates: is there evidence for an adaptive trend?The Journal of experimental biology · 2016Review
- The Primary Structure of β(I)-Chain of Hemoglobin from Snake Sindhi Krait (Bungarus sindanus sindanus).The protein journal · 2016Article
- Gene Duplication and Evolutionary Innovations in Hemoglobin-Oxygen Transport.Physiology (Bethesda, Md.) · 2016Review
- Convergent Evolution of Hemoglobin Function in High-Altitude Andean Waterfowl Involves Limited Parallelism at the Molecular Sequence Level.PLoS genetics · 2015Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Available data suggest that snake hemoglobins (Hbs) are characterized by a combination of unusual structural and functional properties relative to the Hbs of other amniote vertebrates, including oxygenation-linked tetramer-dimer dissociation. However, standardized comparative data are lacking for snake Hbs, and the Hb isoform composition of snake red blood cells has not been systematically characterized. Here we present the results of an integrated analysis of snake Hbs and the underlying α- and β-type globin genes to characterize 1) Hb isoform composition of definitive erythrocytes, and 2) the oxygenation properties of isolated isoforms as well as composite hemolysates. We used species from three families as subjects for experimental studies of Hb function: South American rattlesnake, Crotalus durissus (Viperidae); Indian python, Python molurus (Pythonidae); and yellow-bellied sea snake, Pelamis platura (Elapidae). We analyzed allosteric properties of snake Hbs in terms of the Monod-Wyman-Changeux model and Adair four-step thermodynamic model. Hbs from each of the three species exhibited high intrinsic O2 affinities, low cooperativities, small Bohr factors in the absence of phosphates, and high sensitivities to ATP. Oxygenation properties of the snake Hbs could be explained entirely by allosteric transitions in the quaternary structure of intact tetramers, suggesting that ligation-dependent dissociation of Hb tetramers into αβ-dimers is not a universal feature of snake Hbs. Surprisingly, the major Hb isoform of the South American rattlesnake is homologous to the minor HbD of other amniotes and, contrary to the pattern of Hb isoform differentiation in birds and turtles, exhibits a lower O2 affinity than the HbA isoform.
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