Mole Rat Hemoglobin: Primary Structure and Evolutionary Aspects in a Second Karyotypeof Spalax ehrenbergi,Rodentia, (2n = 52)
- 1 January 1985
- journal article
- research article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 366 (2) , 679-686
- https://doi.org/10.1515/bchm3.1985.366.2.679
Abstract
The Hb of the 4 karyotypes of S. ehrenbergi (2n = 52, 54, 58, 60) did not show any differences in their electrophoretic pattern and in high performance liquid chromatography. The complete amino-acid sequence of mole rat Hb (S. ehrenbergi), chromosome species 2n = 52, is presented. It was elucidated by automatic Edman degradation of the chains, the tryptic peptides and the C-terminal peptide obtained by acid hydrolysis of the Asp.sbd.Pro bond in .beta.-chains. The .alpha.- and .beta.-chains are identical with those of the chromosome species 2n = 60. A comparison of the Hb of mole rat, mouse and other rodents shows homology but no indication of adaptation to subterranean life. In all probability .alpha.1 1(A9)Arg and .alpha.1 20(H3)Gly, unique in mole rat among all mammalian Hb, are not involved in high O affinity. The construction of a phylogenetic tree by the maximum parsimony method, based on Hb sequences, made it possible to show that Rodentia originated as a monophyletic clade and to find the phylogenetic relationship of Spalacidae to other Rodentia (Mus, rattus, Ondatra, Mesocricetus, Citellus and Cavia). Among all rodents the slowest rate of nucleotide replacements occurred in the lineage to Spalax (20%) and the fastest in the lineage to Cavia (59%).This publication has 17 references indexed in Scilit:
- The Primary Structure of the Hemoglobin of the Dogfish Shark(Squalus acanthias).Antagonistic Effects of ATP and Urea on Oxygen Affinity of an Elasmobranch HemoglobinBiological Chemistry Hoppe-Seyler, 1985
- The Primary Structure of the Hemoglobin of the Mole Rat(Spalax ehrenbergi,Rodentia, Chromosome Species 60)Hoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1984
- Evolution of cytochromec investigated by the maximum parsimony methodJournal of Molecular Evolution, 1981
- Decoding the pattern of protein evolutionProgress in Biophysics and Molecular Biology, 1981
- Adaptive Convergence and Divergence of Subterranean MammalsAnnual Review of Ecology and Systematics, 1979
- The primary structure of the hemoglobin β-chain of Microtus xanthognathusComparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1977
- HYBRIDIZATION AND SPECIATION IN FOSSORIAL MOLE RATSEvolution, 1976
- Primary sequence of the β-chain of badger haemoglobinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2·5 Å resolution: Refinement of the atomic modelJournal of Molecular Biology, 1975
- Hemoglobins of mice: Sequence and possible ambiguity at one position of the alpha chainJournal of Molecular Biology, 1967