Abstract
The primary structures of the alpha chains in hemoglobins from three stocks of mice with theHba w2,Hba w3, andHba w4 haplotypes were determined to establish whether the tentative alpha-chain assignments based on the results of isoelectric focusing patterns were correct. TheseHba haplotypes were identified in laboratory descendants of feral mice captured in different parts of the world. Hemoglobin from “Centreville,” Maryland,Mus musculus domesticus (Hba w2) contains equal amounts of alpha chains 1 and 3. Hemoglobin from “Czech”Mus musculus musculus (Hba w4) contains equal amounts of alpha chains 3 and 4. Amino acid analysis of the alpha-globins of “Skive” DanishMus musculus musculus (Hba w3) establishes that its hemoglobin is comprised of about one-third alpha chain 2 as expected plus a greater amount of a unique alpha chain that has not been described previously. This unique alpha chain has glycine at position 25, isoleucine at position 62, and serine at position 68; it is called chain 7. It may represent an intermediate in the evolution of genes that code for chain 2 (which has glycine, valine, and serine at positions 25, 62, and 68, respectively) and chain 4 (which has valine, isoleucine, and serine at positions 25, 62, and 62, respectively).
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Erhart, M. A., Piller, K., and Weaver, S. (1987). Polymorphism and gene conversion in mouse α-globin haplotypes.Genetics 115511.
Fitch, W. M. (1974). A comparison between evolutionary substitutions and variants in human hemoglobins.Ann. N.Y. Acad. Sci. 241440.
Hilse, K., and Popp, R. A. (1968). Gene duplication as the basis for amino acid ambiguity in the alpha-chain polypeptides of mouse hemoglobins.Proc. Natl. Acad. Sci. USA 61930.
Jones, R. T. (1964). Structural studies of aminoethylated hemoglobin by automatic peptide chromatography.Cold Spring Harbor Symp. Quant. Biol. 29297.
Lyon, M. F., Barker, J. E., and Popp, R. A. (1988). Mouse globin gene nomenclature.J. Hered. (in press).
Popp, R. A. (1962). Studies on the mouse hemoglobin loci. IV. Independent segregation ofHb andSol: Effect of the loci on the electrophoretic and solubility properties of hemoglobins.J. Hered. 5377.
Popp, R. A. (1965). The separation and amino acid composition of the tryptic peptides of the α chain of hemoglobin of C57BL mice.J. Biol. Chem. 2402863.
Popp, R. A. (1967). Hemoglobins of mice: Sequence and possible ambiguity at one position of the alpha chain.J. Mol. Biol. 279.
Popp, R. A., Bailiff, E. G., Skow, L. C., and Whitney, J. B., III (1982). The primary structure of genetic variants of mouse hemoglobin.Biochem. Genet. 20199.
Popp, R. A., D'Surney, S. J., and Wawrzyniak, C. J. (1987). Changes in expression of murine alpha- and beta-globin genes during development. In Stamatoyannopoulos, G., and Nienhuis, A. (eds.),Fifth Conference on Hemoglobin Switching Alan R. Liss, New York
Russell, E. S., and McFarland, E. C. (1974). The genetics of mouse hemoglobins.Ann. N.Y. Acad. Sci. 24125.
Sack, J. S. Andrew, L. C., Magnus, K. A., Hanson, J. C. Rubin, J., and Love, W. E. (1978). Location of amino acid residues in human hemoglobin.Hemoglobin 2153.
Sage, R. D., Whitney, J. B., III, and Wilson, A. C. (1986). Genetic analysis of a hybrid zone between domesticus and musculus mice (Mus musculus complex): Hemoglobin polymorphisms.Curr. Top. Microbiol. Immunol. 12775.
Schroeder, W. A., Jones, R. T., Cormick, J., and MaCalla, K. (1962). Chromatographic separation of peptides on ion exchange resins.Anal. Chem. 341570.
Vogel, F. (1972). Non-randomness of base replacements in point mutations.J. Mol. Evol. 1334.
Whitney, J. B., III (1986). Immobilized-gradient isoelectric focusing: Detection of “silent” biochemical genetic variants.Curr. Top. Microbiol. Immunol. 127131.
Whitney, J. B., III, Copeland, G. T., Skow, L. C., and Russell, E. S. (1979). Resolution of products of the duplicated hemoglobin α-chain loci by isoelectric focusing.Proc. Natl. Acad. Sci. USA 76867.
Whitney, J. B., III, Cobb, R. R., Popp, R. A., and O'Rourke, T. W. (1985). Detection of neutral amino acid substitutions in proteins.Proc. Natl. Acad. Sci. USA 827646.
Wilson, S., and Smith D. B. (1959). Separation of the valyl-leucyl and valyl-glutamyl polypeptide chains of horse globin by fractional precipitation and column chromatography.Can. J. Biochem. Physiol. 37405.
Author information
Authors and Affiliations
Additional information
This research was sponsored jointly by the National Institutes of Environmental Health Sciences under Contract 1-ES-55078 and by the Office of Health and Environmental Research, U.S. Department of Energy, under Contract DE-AC05-840R21400 with Martin Marietta Energy Systems, Inc.
Rights and permissions
About this article
Cite this article
Popp, R.A., Comer, K.A., Cobb, R.R. et al. A unique alpha chain in hemoglobin of “Skive” DanishMus musculus . Biochem Genet 26, 1–8 (1988). https://doi.org/10.1007/BF00555484
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00555484