Isolation, characterization and N-terminal amino-acid sequence of rabbit transferrin.
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.
Godovac-Zimmermann
J
J
John Curtin School of Medical Research, Department of Biochemistry, Australian National University, Canberra City.
D000595:Amino Acid Sequence; D000818:Animals; D001322:Autoanalysis; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D008969:Molecular Sequence Data; D011817:Rabbits; D014168:Transferrin / Q000302:isolation & purification
D014168:Transferrin