Isolation, characterization and N-terminal amino-acid sequence of rabbit transferrin |
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| Authors: | J Godovac-Zimmermann |
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| Affiliation: | John Curtin School of Medical Research, Department of Biochemistry, Australian National University, Canberra City. |
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| Abstract: | Rabbit serum transferrin has been isolated and purified by ion-exchange column and high-performance liquid chromatography. The N-terminal amino-acid sequence of 32 residues was determined by automatic Edman degradation in a liquid phase sequenator. Of the first twelve residues sequenced previously three identifications were corrected. Comparison with the known transferrin sequences shows 15 common amino-acid residues. Comparison to human serum transferrin revealed that 37% of amino-acid residues were exchanged. Cys9 and Cys19 which are supposed to be involved in disulphide bridges, are conserved. |
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