Primary structure of hemoglobin beta-chain from Columba livia (gray wild pigeon).
Primary structure of beta-chain of pigeon is presented. It was determined by amino acid sequence analysis of intact beta-chain and its peptides obtained by the enzymatic and chemical cleavage. Comparison of amino acid sequence of the chain with other available data shows beta 14 Ile, beta 61 Lys, and beta 113 Ile as residues specific to pigeon. One important replacement at alpha 1 beta 1 contact is beta 55 Met----Ser.
HEJ Research Institute of Chemistry, University of Karachi, Pakistan.
C
C
Sultana
A
A
Abbasi
Z H
ZH
Zaidi
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D010856:Columbidae / Q000097:blood*; D005914:Globins / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid; D014357:Trypsin
D010446:Peptide Fragments; D005914:Globins; D014357:Trypsin