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Influence of Low Cetyltrimethylammonium Bromide Concentration on the Interactions and Properties of Hemoglobin with Acyclovir
Author(s) -
Liu TianQing,
Guo Rong
Publication year - 2006
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200690119
Subject(s) - chemistry , zeta potential , bromide , hemoglobin , fluorescence , absorption (acoustics) , conductivity , absorption spectroscopy , nuclear chemistry , transmission electron microscopy , hemeprotein , analytical chemistry (journal) , photochemistry , inorganic chemistry , chromatography , organic chemistry , chemical engineering , heme , nanoparticle , physics , quantum mechanics , acoustics , engineering , enzyme
The effects of cetyltrimethylammonium bromide (CTAB) on the properties of hemoglobin (Hb) at low CTAB concentration were studied in Hb/acyclovir/CTAB system by the methods of UV‐Vis spectrum, fluorescence, zeta potential, conductivity and negative‐staining transmission electron microscope (TEM). With the increase of CTAB concentration, the UV peak intensity at 276 nm, the intrinsic fluorescence, the zeta potential of Hb and the system conductivity were all enhanced. Hb was easily oxidized to oxyHb and hemichrome. In Hb/acyclovir/CTAB system, CTAB made the UV‐Vis spectrum, fluorescence, conductivity and conformation of Hb tend to be returned to those of the original Hb but the zeta potential not to do so. The UV absorption peak of Hb‐acyclovir complex disappeared, and the tight structure of Hb aroused by acyclovir was refolded. When CTAB concentration was higher than 5×10 −5 mol/L, the two absorption peaks at 536 and 576 nm appeared again, and the Hb structure became looser again.