Heterogeneity and subunit composition of the haemoglobins of five tilapiine species (Teleostei, Cichlidae) of the genera Oreochromis and Sarotherodon |
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Authors: | T M Falk W Villwock L Renwrantz |
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Institution: | Zoologisches Institut und Zoologisches Museum, Universit?t Hamburg, Martin-Luther-King-Platz 3, D-20146 Hamburg, Germany Fax: +49 40 4123 3937, e-mail: tmfalk@pin-net.de, DE
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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.
Accepted: 12 September 1997 |
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Keywords: | Haemoglobins Globin chains Subunit structures β -chain sequences Tilapias |
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