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Sphingomyelin-induced structural modification of Human Hemoglobin (Hb) has been investigated in its native and unfolded conformers that are partially denatured in presence of ∼ 4 M urea, completely denatured in ∼ 8 M urea and thermally disrupted (at ∼ 65 °C) state. The absorption studies unveil ground state complexation between Hb and SM. From steady-state fluorescence and quenching studies alteration of the micro-environments around Trp residues of Hb in above mentioned different cases has been determined. Moreover, lesser exposure of
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