Mouse Hemoglobin

Oxygen Binding Dynamics

• P₅₀ (mmHg):

  • Hbb^maj: 14.8 ± 0.4

  • Hbb^s: 13.3 ± 0.6

  • Hbb^min: 13.6 ± 0.5

• Hill coefficient (n): 2.45–2.59 (vs. 2.8–3.0 in humans)

• Alkaline Bohr effect:

  • Hbb^maj: 0.69

  • Hbb^s: 0.61

  • Hbb^min: 0.60

Red Blood Cell (RBC) Oxygenation

Stability Profiles

Mouse hemoglobin variants show differential resistance to denaturation:

• Mechanical stability (kinetic constant k):

  • Hbb^maj: 0.098 ± 0.01/min

  • Hbb^s: 0.027 ± 0.013/min

  • Hbb^min: 0.27/min

• Heat stability: All mouse hemoglobins are less stable than human HbA or HbS .

HbSC Disease Mimicry

A transgenic HbSC mouse model replicates human sickle cell disease features:

• Key findings:

  • RBC dehydration (↑ mean corpuscular hemoglobin concentration)

  • Hypoxia-induced membrane damage

  • Retinopathy and organ damage despite reduced hemolysis vs. HbSS mice

• Clinical relevance: Enables targeted therapy development for HbSC patients .

Detection and Measurement

ELISA quantification (ab254517 kit):

Research Implications

• Transgenic studies: Mouse hemoglobin polymorphisms (e.g., Hbb^maj/Hbb^min) aid in modeling human hemoglobinopathies .

• Hematological recovery: Weekly 15–25% blood volume collection in C57BL/6 mice shows rapid RBC regeneration (hemoglobin normalization within 7 days) .