Influences of Triton X‐100 on Hemoglobin Behaviors in Hemoglobin/Acyclovir/Triton X‐100/H₂O System

The influences of Triton X‐100 on hemoglobin (Hb) behaviors were studied by the methods of UV‐Vis spectrum, fluorescence spectrum, HPLC, conductivity, zeta potential and negative‐staining transmission electron microscope in Hb/acyclovir/Triton X‐100/H 2 O system. With the increase of Triton X‐100 concentration in the system, the percentage of the free acyclovir increased from 58%–63% to 90%–94%. The static quenching constant and the association number of acyclovir to Hb decreased. The fluorescence spectrum, conductivity, zeta potential, fluorescence polarization and negative‐staining morphology of Hb tended to recover to those of the original state of Hb in the same concentration of Hb. The interaction between Triton X‐100 and Hb is stronger than that between acyclovir and Hb. Most Triton‐X‐100 was associated with Hb at low Triton X‐100 concentration. But the interaction of Triton X‐100 with Hb was apparently dominant in high Triton X‐100 concentration. The Hb structure was unfolded and finally denatured.