PMID: 2124278Oct 1, 1990Paper

Discrimination between adaptive and neutral amino acid substitutions in vertebrate hemoglobins

Journal of Molecular Evolution
K HorimotoJ Otsuka

Abstract

A discriminant analysis on the basis of the physicochemical properties of amino acid residues is developed to investigate the accumulation pattern of amino acid substitutions in a family of proteins. The application of this analysis to vertebrate hemoglobins reveals the following new results. (1) The major components of teleost fish and amphibian hemoglobins showing the Root effect are sharply discriminated from mammalian hemoglobins in several regions of the alpha and beta chains, whereas shark, minor components of teleost fish and amphibian, reptile, and bird hemoglobins showing no Root effect exhibit a gradual change to mammalian hemoglobin in a straightforward way. This result suggests at least two lines of molecular evolution in vertebrate hemoglobins. (2) The nonadult hemoglobin chains are allocated to the latter line, i.e., tadpole, zeta, and pi chains are similar to shark and trout I chains, and epsilon and gamma chains are similar to some of the reptile chains. (3) In any case, most of the amino acid residues causing the discrimination are located near the sites that carry the amino acid residues conserved well throughout all classes of vertebrates, suggesting that modifications adapting to the respective living condit...Continue Reading

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Citations

Sep 1, 1994·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·R J MacIntyre
May 20, 2015·Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP·Halina FalfushynskaRostyslav Stoika
Mar 1, 1996·Nature Structural Biology·S E MylvaganamE D Getzoff
Oct 20, 2004·Acta Physiologica Scandinavica·C BonaventuraR E Weber

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