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  • 1
    Electronic Resource
    Electronic Resource
    Hematology of a Murine β-Thalassemia: A Longitudinal Study (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 445 (1985), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1985.tb17213.x
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  • 2
    Electronic Resource
    Electronic Resource
    Primary structure of two nonallelicβ-globin chains from DBA/2 mice (1987)
    Springer
    Biochemical genetics 25 (1987), S. 391-399 
    Details
    ISSN: 1573-4927
    Keywords: amino acid sequence ; protein evolution ; inbred mice ; β major and β minor globin ; murine erythroleukemia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The amino acid sequences of the β major and β minor globin chains from DBA/2 mice have been determined. This information is of interest because DBA/2 mice are the strain of origin for most murine erythroleukemia lines. The primary structure of DBA/2 β globins agrees completely with that predicted from the coding properties of BALB/c β globin genes. This identity does not support a rapid evolutionary divergence in inbred mouse strains, at least at these loci in these strains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554548
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  • 3
    Electronic Resource
    Electronic Resource
    A unique alpha chain in hemoglobin of “Skive” DanishMus musculus (1988)
    Springer
    Biochemical genetics 26 (1988), S. 1-8 
    Details
    ISSN: 1573-4927
    Keywords: feral mouse hemoglobins ; alpha-chain structure ; Hba haplotypes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: 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).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00555484
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  • 4
    Electronic Resource
    Electronic Resource
    Independent expression of the two mouse adult β-globin genes (1986)
    Springer
    Biochemical genetics 24 (1986), S. 259-272 
    Details
    ISSN: 1573-4927
    Keywords: mice ; β-minor and β-major globin ; dot blot hybridization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Dot blot hybridization was used to determine the relative amounts of the β-major and β-minor globin RNAs present in reticulocytes of mice at 14.5 and 17.5 days of gestation, newborns, and adults of the Hba b /Hba b ;Hbb s2 /Hbb s2 globin genotype. RNAs isolated from embryonic yolk sac, fetal liver, and adult reticulocytes were hybridized with the following labeled DNA probes: α-1, β-minor specific, and β-major specific. The level of β-sminor RNA in reticulocytes at 14.5 and 17.5 days of gestation is nearly the same as in induced reticulocytes of adult mice. In contrast, the level of β-s2major RNA in reticulocytes at 14.5 days of gestation is 0.23× and at 17.5 days of gestation is 0.66× the amount found in reticulocytes of adult mice. These results correlate well with earlier observations that the β-sminor globin gene approaches its normal adult level of expression by 14.5 days of gestation, whereas the β-s2major globin gene expression increases between 14.5 days of gestation and 6 days postnatally. They indicate that the differential expression of β-sminor and β-s2major globins during development is regulated at the level of transcription. Expression of the β-minor globin gene in reticulocytes of adult normal mice is not maximal, however, because the levels of the β-minor globin and its RNA are increased further in reticulocytes of thalassemic mice.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00502793
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  • 5
    Electronic Resource
    Electronic Resource
    The primary structure of genetic variants of mouse hemoglobin (1982)
    Springer
    Biochemical genetics 20 (1982), S. 199-208 
    Details
    ISSN: 1573-4927
    Keywords: mouse hemoglobin ; neutral amino acid substitution ; isoelectric focusing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The primary structures of the α globins from CE/J, DBA/2J, and a stock of Potter's mice were determined to identify the amino acid substitutions associated with the unique isoelectric focusing patterns of these hemoglobins. In addition, the primary structures of the α globins from MOL III and PERU mice were studied in search of amino acid substitutions that may not be detected by isoelectric focusing. CE/J hemoglobin contains a unique kind of α globin called chain 5. It differs from the single kind of α globin (chain 1) in C57BL/6 by having alanine rather than glycine at position 78. DAB/2J hemoglobin has two kinds of α globins: one half is like chain 5 and the other half is like chain 1. The hemoglobin from Potter's stock of Mus musculus molossinus also contains chains 1 and 5, but they are expressed at different levels, i.e., 80% chain 1 and 20% chain 5. MOL III hemoglobin has a single kind of α globin identical to that in C57BL/6, and PERU hemoglobin contains approximately 40% chain 1 and 60% chain 4. Chains 1 and 4 have different amino acids at positions 25, 62, and 68. These studies confirm that mouse hemoglobins separable by isoelectric focusing, but not by other means of electrophoresis, have substitutions of neutrally charged amino acids in their α chains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484946
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