Crystal structure of hemoglobin from mouse (Mus musculus) compared with those from other small animals and humans.

ABSTRACT: Mice (Mus musculus) are nocturnal small animals belonging to the rodent family that live in burrows, an environment in which significantly high CO₂ levels prevail. It is expected that mouse hemoglobin (Hb) plays an important role in their adaptation to living in such a high-CO₂ environment, while many other species cannot. In the present study, mouse Hb was purified and crystallized at a physiological pH of 7 in the orthorhombic space group P2₁2₁2₁; the crystals diffracted to 2.8 Å resolution. The primary amino-acid sequence and crystal structure of mouse Hb were compared with those of mammalian Hbs in order to investigate the structure-function relationship of mouse Hb. Differences were observed from guinea pig Hb in terms of amino-ac

SUBMITTER: Sundaresan SS 

PROVIDER: S-EPMC8034429 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature