| extensive gross genomic rearrangements between chicken and old world vultures (falconiformes: accipitridae). | the karyotypes of most birds consist of a small number of macrochromosomes and numerous microchromosomes. intriguingly, most accipitrids which include hawks, eagles, kites, and old world vultures (falconiformes) show a sharp contrast to this basic avian karyotype. they exhibit strikingly few microchromosomes and appear to have been drastically restructured during evolution. chromosome paints specific to the chicken (gga) macrochromosomes 1-10 were hybridized to metaphase spreads of three species ... | 2006 | 16484785 |
| high altitude and hemoglobin function in the vultures gyps rueppellii and aegypius monachus. | functional characteristics of the stripped composite hemoglobins (hbs) of the vultures gyps rueppellii and aegypius monachus that can fly at extremely high altitudes, and of component hbs of g. rueppellii are reported, in relation to influences of ph, temperature and inositol hexaphosphate. g. rueppellii hbs a, a' and d represent a sequence of increasing oxygen affinity, which is opposite to earlier results on avian hb components, but correlates with two alpha-chain substitutions that predictabl ... | 2012 | 3401328 |
| [molecular aspects of high altitude respiration of birds. hemoglobins of the striped goose (anser indicus), the andean goose, (chloephaga melanoptera) and vulture (gyps rueppellii)]. | respiration of birds at high altitude and the structural adaptation of avian hemoglobins are studied. applying the method of the "minimal biological distance", hemoglobins of closely related species were sequenced and compared with each other. physiological measurements and sequence data show that adaptation to hypoxic stress can be interpreted as exchange of one amino acid. the structural aspects of the genetical data are discussed on the basis of the atomic model of hemoglobin. high-altitude r ... | 1988 | 3205309 |
| high-altitude respiration of birds. structural adaptations in the major and minor hemoglobin components of adult rüppell's griffon (gyps rueppellii, aegypiinae): a new molecular pattern for hypoxic tolerance. | the primary structures of the hemoglobins hb a, hb a', hb d and hb d' of rüppell's griffon (gyps rueppellii), which can fly as high as 11,300 m, are presented. the globin chains were separated on cm-cellulose in 8m urea buffers, the four hemoglobin components by fplc in phosphate buffers. the amino-acid sequences of five globin chains were established by automatic edman degradation of the globin chains and of the tryptic peptides in liquid-phase and gas-phase sequenators. the sequences are compa ... | 1988 | 3401327 |