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  • hemoglobin  (2)
  • Springer  (2)
  • 1975-1979  (2)
  • 1
    ISSN: 1573-4927
    Keywords: crustacean ; hemoglobin ; polyacrylamide electrophoresis ; Artemia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two loci account for all genetic variation resulting in difference in electrophoretic mobility in three hemoglobins (Hb1, Hb2, and HbX) in the hemolymph of the brine shrimp. Four α alleles and nine β alleles have been studied. In shrimps of all genotypes and in electrophoresis in media with varying degrees of molecular sieving, Hb2 is approximately equidistant from Hb1 and HbX. A shrimp heterozygous at both loci has a three-banded Hb1, a four-banded Hb2, and a three-banded HbX. We conclude that Hb2 contains n α-polypeptides and n β-polypeptides. Hb1 contains 2n α-polypeptides. HbX contains 2n β-polypeptides. During electrophoresis, the three native hemoglobins undergo reversible dissociation to n subunits. Subunits with the same charge reassemble to migrate as molecules of the same size as the native molecules. Although there is no evidence for an additional polypeptide in the three hemoglobins, we cannot exclude such a possibility. If it exists, it is under three constraints: (1) it must be present in equal amounts in each of the three hemoglobins; (2) it must have the same molecular weight as the α- and β-polypeptides; and (3) it must be free of genetic variation (detectable by electrophoresis).
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 15 (1977), S. 423-437 
    ISSN: 1573-4927
    Keywords: hemoglobin ; polyacrylamide electrophoresis ; crustacean ; Artemia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Electrophoretic mobilities of three hemoglobins (Hb1, Hb2, and Hb3) were studied in 15 populations of brine shrimps. Genetic segregation data support the model that Hb2 contains n α-polypeptides and n β-polypeptides; Hb1 contains 2n α-polypeptides. Hb3 contains neither α- nor β-polypeptides. There is no evidence of linkage of α and β loci with each other or with the locus (or loci) which governs Hb3 or with the nonhomologous portion of the sex chromosomes. Hemoglobins of different populations may be hybridized in vitro by incubation at high temperature. Reversible dissociation to subunits which contain only one (α or β) polypeptide occurs at 40 C (for Hb1) and at 50 C (for Hb2).
    Type of Medium: Electronic Resource
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