Primary structure of hemoglobin alpha-chain from cuckoo (Eudynamys scolopaceae, cuculiformes).
The complete amino acid sequence of the alpha A-chain of major hemoglobin component from Cuckoo (Eudynamys scolopaceae) is presented. Separation of the polypeptide subunits was achieved by ion exchange chromatography in the presence of 8 M urea. The sequence was studied by automatic Edman degradation of the native chain and its tryptic fragments in a gas-phase sequencer. Comparison with other avian hemoglobins shows residues alpha 21, alpha 30, alpha 96, alpha 110, and alpha 114 as being specific to Cuckoo. The functional significance of these is discussed.
HEJ Research Institute of Chemistry, University of Karachi, Pakistan.
A
A
Abbasi
Z H
ZH
Zaidi
D000595:Amino Acid Sequence; D000818:Animals; D001717:Birds / Q000097:blood*; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005914:Globins / Q000737:chemistry*; D006441:Hemoglobin A / Q000737:chemistry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D014357:Trypsin
D010446:Peptide Fragments; D005914:Globins; D006441:Hemoglobin A; D014357:Trypsin