Prosimian hemoglobins--V. The primary structures of the alpha-I, alpha-II and beta-hemoglobin chains of Hapalemur griseus, with a note on the classification of Microcebus.
1. The duplicated adult hemoglobins were isolated from a mature Hapalemur griseus and the constituent chains prepared. Sequence analysis of the isolated alpha-globins showed that the alpha-I and alpha-II chains differed by a glycine for lysine substitution at position 15. 2. The complete amino acid sequence of the single adult beta-globin of Hapalemur griseus was determined. The beta-globin sequence of Hapalemur griseus clusters with those of other authentic lemurs, and is clearly separated from the sequences characteristic of lorisiform primates. 3. Partial sequence analysis of the beta-globin of Microcebus murinus showed only a single amino acid difference when compared to the Hapalemur globin. 4. Partial sequence analysis of the alpha-globin of Microcebus murinus showed only three amino acid residues that are not found in other lemuriform alpha-globins; two of these are unique to Microcebus among all known prosimian alpha-globin sequences. 5. The Microcebus alpha- and beta-globins are more similar to the homologous lemuriform sequences than they are to lorisiform sequences.
Duffy
L K
LK
Department of Chemistry, University of Alaska Fairbanks 99775-0180.
Luick
J
J
Coppenhaver
D H
DH
D000595:Amino Acid Sequence; D000818:Animals; D005914:Globins / Q000737:chemistry; D006454:Hemoglobins / Q000737:chemistry*; D007900:Lemur / Q000097:blood; D007901:Lemuridae / Q000097:blood / Q000145:classification; D008969:Molecular Sequence Data; D013045:Species Specificity; D011443:Strepsirhini / Q000097:blood*
D006454:Hemoglobins; D005914:Globins