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- W2086953552 abstract "Abstract 1. 1. The over 300 adult individuals of the European eel, Anguilla anguilla (L.), examined showed the same electrophoretic pattern of the hemoglobins; the 293 juvenile individuals were found to be monomorphic too. 2. 2. The hemoglobin system of the adult individuals includes an acidic (anodic) component and two basic (cathodic) components, a major one and a minor one. 3. 3. Both the acidic component and the major basic component, separated by electrophoresis or by ion-exchange chromatography and analyzed by 8 M urea electrophoresis, were found to be symmetrical heterotetramers. 4. 4. By means of isoelectric focusing a higher multiplicity is obtained, but the polypeptide constitution of the focused fractions is the same we found with the previous methods: the higher multiplicity should depend on associations with the polyampholytes. 5. 5. The molecular weights of the polypeptides have been compared by means of SDS—urea electrophoresis, while the acidic component seems almost normal, in the basic component the β polypeptide were found to be lighter than the α polypeptide. 6. 6. These polypeptides have been attributed to the classes α and β by digestion with carboxypeptidases A and B." @default.
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- W2086953552 date "1987-01-01" @default.
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- W2086953552 title "The hemoglobins of Anguilla anguilla (L.)—II. Polypeptide constitution" @default.
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- W2086953552 doi "https://doi.org/10.1016/0305-0491(87)90168-4" @default.
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