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  • Globin chains  (2)
  • Anodonta cygnea  (1)
  • Biomphalaria glabrata  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Invertebrate Pathology 46 (1985), S. 209-210 
    ISSN: 0022-2011
    Keywords: Achatina fulica ; Anodonta cygnea ; Biomphalaria glabrata ; Crassostrea gigas ; Cytotoxic molecules ; Helix pomatia ; Hemocytes, molluscan ; Lymnaea stagnalis ; Mytilus edulis ; Unio pictorum
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-143X
    Keywords: Genetic variation ; Globin chains ; Haemoglobins ; Species differentiation ; Tilapia (Oreochromis, Sarotherodon, Tilapia)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Haemoglobins of ten tilapia species of the genera Oreochromis, Sarotherodon and Tilapia, three subspecies of the Nile tilapia, O. niloticus, and an artificial hybrid cross were analysed by isoelectric focusing aimed at characterizing the taxonomic value of these oxygen-binding molecules. Heterogeneous haemoglobin phenotypes were observed in haemolysate samples of all the fishes, and species-characteristic as well as subspecies-characteristic patterns could be identified. F1 hybrids were distinguishable from pure parental specimens. Globin chain studies by AU- and AUT-PAGE systems confirmed the heterogeneity and species specificity observed by isoelectric focusing of the tetrameric molecules. A total of eight different α-chains and eight different β-chains were detected by AU-PAGE and species-characteristic globin chain variants were shown to occur in almost all species. Globin chain profiles of hybrid specimens were characterized by the presence of all parental globin chain variants. © Rapid Science Ltd. 1998
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-136X
    Keywords: Key words Haemoglobins ; Globin chains ; Subunit structures ; β-chain sequences ; Tilapias
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Haemoglobins of five tilapiine species of the genera Oreochromis and Sarotherodon were investigated. By gel filtration chromatography a molecular weight of 67–69 kDa was determined for the tetrameric molecules which remained stable between pH 5.0 and pH 9.1. When subjected to sodium dodecyl sulphate-Urea-polyacrylamide gel electrophoresis (PAGE), haemoglobins of all species each were split into monomers of three different molecular weights ranging between 16.3 kDA and 17.6 kDa. Subsequently, isoelectric focusing separated haemolysates into about 23 differently charged tetrameric haemoglobins that were arranged in species-specific patterns. This diversity was shown to result from the occurrence of different types of globin chains. By acidic urea PAGE a total of seven major α-globins and five major β-globins were detected and species-characteristic chain variants were identified. To determine the globin chain composition of particular haemoglobin tetramers, 26 bands were isolated by isoelectric focusing and analysed by acidic urea PAGE. Tetramers consisted of doublets of identical α- and identical β-chains (α2β2, symmetric tetramers), or combinations of three (α2ββ*; αα*β2) or four (αα*ββ*) distinct chains (asymmetric tetramers). Finally, globin chains of Oreochromis niloticus were subjected to partial N-terminal amino acid sequencing. Differences in the composition of the three major β-chains could be shown, whereas the α-chains were N-terminally blocked.
    Type of Medium: Electronic Resource
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