The primary structure of adult hemoglobin of musk shrew (Suncus murinus).
An alpha chain and two beta chains beta I and beta II) were obtained from adult hemoglobin of the musk shrew (Suncus murinus) by CM-cellulose column chromatography. The S-carboxymethylated alpha chain and the S-aminoethylated beta chains were each digested with trypsin and the amino acid sequences of the tryptic peptides obtained were established. The ordering of these peptides in the alpha and beta chains was deduced from their homology with the primary structures of the alpha and beta chains of human adult hemoglobin. The sequence of the alpha chain thus determined indicated to be heterogeneous at the 15th position from the N-terminus. On the other hand, comparing the primary structure of beta I chain with that of beta II chain, 4 amino acid exchanges were recognized. Further, the primary structures of the alpha and beta chains of musk shrew hemoglobin were compared with those of alpha and beta chains of human and European hedgehog hemoglobins.
D000595:Amino Acid Sequence; D000818:Animals; D006441:Hemoglobin A / Q000302:isolation & purification; D006801:Humans; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D012788:Shrews / Q000097:blood*; D013045:Species Specificity; D014357:Trypsin
D046911:Macromolecular Substances; D010446:Peptide Fragments; D006441:Hemoglobin A; D014357:Trypsin