Amino acid sequences of hemoglobin from guinea fowl (Numida meleagri) and California quail (Lophortyx californica) with phylogenetic analysis of major groups of Galliformes.
We determined the complete amino acid sequences of the hemoglobin of two species, guinea fowl and California quail, in Galliformes from intact globin chain and chemical cleavage fragments in order to analyze the molecular evolution of hemoglobin for the classification of Galliformes. Galliformes have two types of hemoglobin components, HbA and HbD, which consist of identical beta chain and different alpha chains. The sequences are similar to globin chains of Galliformes reported previously. These sequences were compared with those of other Galliformes (Phasianidae, Meleagrididae) using duck and goshawk as out-groups. The phylogenetic tree of major groups of Galliformes based on hemoglobin was similar to the tree model produced based on the amino acid sequence of lysozyme c.
Eguchi
Y
Y
Research Laboratory Center, Faculty of Medicine, University of the Ryukyus, Okinawa, Japan. yeguchi@med.u-ryukyu.ac.jp
Ikehara
T
T
Eguchi
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001717:Birds / Q000145:classification / Q000378:metabolism*; D006454:Hemoglobins / Q000737:chemistry* / Q000145:classification; D008969:Molecular Sequence Data; D010802:Phylogeny; D011784:Quail; D020539:Sequence Analysis, Protein; D017385:Sequence Homology
D006454:Hemoglobins