Cation modulation of hemoglobin interaction with sodium n-dodecyl sulfate (SDS). I: Calcium modulation at pH 7.20.

摘要: We investigate the conformational differences between HbA and HbS in presence absence of Ca2+ concentrations (0–40 μM) akin to those within erythrocyte cytoplasm membrane mimetic native structure disrupting environments Plasmodium parasite food vacuole at pH 5.0. The experiments were monitored by UV–Vis spectrophotometery range 250–650 nm. Our results suggest that HbS, on interacting with both mimic 40 μM Ca2+, undergoes an “expansion” burst phase proteins accompanied tyrosine exposure while occurred tryptophan exposure. flexibility unlike HbA. Besides, spectral also complexes its immediate environment without strain (due inherent flexibility), HbA, thus appropriating cation from vicinity. implications these are discussed light possible mechanisms employed resist protease digestion or least slow down kinetics activities how same factors can predispose homozygous individuals sickling consequent vaso-occlusive crisis.