Rücknagel K P, Wiesner H, Braunitzer G
Max-Planck-Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
Biol Chem Hoppe Seyler. 1990 Jun;371(6):503-9. doi: 10.1515/bchm3.1990.371.1.503.
The primary structures of alpha- and beta-chains from the hemoglobin of the Beach Marten (Martes foina, Carnivora) are presented. The globin chains were separated on CM-cellulose in 8M urea buffer. The amino-acid sequences were established by automatic liquid- and gas-phase Edman degradation of the intact chains and the tryptic peptides from oxidized chains. Comparison of the sequences with human hemoglobin shows 21 exchanges in the alpha- and 12 in the beta-chains. The differences concerning heme and interchain contact sites as well as the substitution alpha 77 (EF6)Pro----Ala are discussed. The latter is observed for the first time in a mammalian hemoglobin. The sequences are compared with those of other Carnivora. The beta-chains of Martes foina and Pteronura brasiliensis (Giant Otter) are found to be identical, but their alpha-chains differ in 7 positions. The surprising small numbers of exchanges between the hemoglobin from Beach marten and that from Lesser and Greater Panda are discussed.
