The Amino Acid Sequences of the α and β Chains of Hemoglobin from the Snake, Liophis Miliaris
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference39 articles.
1. Oxygen dissociation constants in haemoglobins of Helicops modestus and Liophis miliaris, two water-snakes with different morphological adaptations to their aquatic environment
2. Content of organic polyphosphates and their allosteric effects on haemoglobins from the water-snakes Helicops modestus and Liophis miliaris
3. Dimer-tetramer transition in hemoglobins from Liophis miliaris—I. Effect of organic polyphosphates
4. The amino acid sequences of chains a, b, and c that form the trimer subunit of the extracellular hemoglobin from Lumbricus terrestris.
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1. Distribution, adaptation and physiological meaning of thiols from vertebrate hemoglobins;Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology;2007-07
2. The mammalian αD-globin gene lineage and a new model for the molecular evolution of α-globin gene clusters at the stem of the mammalian radiation;Molecular Phylogenetics and Evolution;2006-02
3. The Primary Structure of Three Hemoglobin Chains from the Indigo Snake (Drymarchon corais erebennus, Serpentes): First Evidence for αD Chains and Two β Chain Types in Snakes;Biological Chemistry;2002-12-09
4. ATP-induced Tetramerization and Cooperativity in Hemoglobin of Lower Vertebrates;Journal of Biological Chemistry;1999-01
5. Vertebrate Hemoglobins;Comprehensive Physiology;1997-12
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