AbstractGlucosylated human serum albumin (G-HSA) obtained under incubation with glucose at 37° C for 8 days showed a new fluorescence with a maximum at 430 nm, resulting in quenching of the fluorescence of only one tryptophan residue on HSA. The quantum yield of new fluorescence is 0.024 at 25° C. The analysis of the excitation spectra allowed us to conclude the absence of energy transfer. In G-HSA, non-disulfide cross-linking hexamer was confirmed by SDS-PAGE
When encapsulated by human serum albumin (HSA), certain derivatives of the green. fluorescent protei...
The steady-state and time-resolved studies of the sensitized emission of the excited-state proton tr...
The Human Serum Albumin (HSA) can emit fluorescence (??em=350 nm) under irradiation of ultraviolet l...
AbstractGlucosylated human serum albumin (G-HSA) obtained under incubation with glucose at 37° C for...
AbstractHuman serum albumin (HSA) contains a single tryptophan residue at position 214. The emission...
7-12The binding of monomeric heme to human serum albumin (HSA) was investigated using steady-state f...
The changes in the far-UV CD signal, intrinsic tryptophan fluorescence and bilirubin absorbance show...
<p>The fluorescence spectra of human serum albumin (HSA, 1.5×10<sup>−5</sup> mol/L) (A) in the absen...
AbstractThe interaction between Thioguanine (6-TG) and human serum albumin (HSA) under simulative ph...
Two donor-acceptor fluorophores were prepared and tested for quantitative determination of HSA in aq...
The interaction between a bioactive molecule, 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinoliz...
The molecular origin behind the concentration-dependent intrinsic blue fluorescence of human serum a...
Continuous 295nm excitation of bovine apo-α-lactalbumin (apo-bLA) results in an increase of tryptoph...
The unfolding of human serum proteins (HSP) was studied by measuring the intrinsic fluorescence inte...
This research examines the interaction between human serum albumin (HSA) and various sugar forms (β-...
When encapsulated by human serum albumin (HSA), certain derivatives of the green. fluorescent protei...
The steady-state and time-resolved studies of the sensitized emission of the excited-state proton tr...
The Human Serum Albumin (HSA) can emit fluorescence (??em=350 nm) under irradiation of ultraviolet l...
AbstractGlucosylated human serum albumin (G-HSA) obtained under incubation with glucose at 37° C for...
AbstractHuman serum albumin (HSA) contains a single tryptophan residue at position 214. The emission...
7-12The binding of monomeric heme to human serum albumin (HSA) was investigated using steady-state f...
The changes in the far-UV CD signal, intrinsic tryptophan fluorescence and bilirubin absorbance show...
<p>The fluorescence spectra of human serum albumin (HSA, 1.5×10<sup>−5</sup> mol/L) (A) in the absen...
AbstractThe interaction between Thioguanine (6-TG) and human serum albumin (HSA) under simulative ph...
Two donor-acceptor fluorophores were prepared and tested for quantitative determination of HSA in aq...
The interaction between a bioactive molecule, 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinoliz...
The molecular origin behind the concentration-dependent intrinsic blue fluorescence of human serum a...
Continuous 295nm excitation of bovine apo-α-lactalbumin (apo-bLA) results in an increase of tryptoph...
The unfolding of human serum proteins (HSP) was studied by measuring the intrinsic fluorescence inte...
This research examines the interaction between human serum albumin (HSA) and various sugar forms (β-...
When encapsulated by human serum albumin (HSA), certain derivatives of the green. fluorescent protei...
The steady-state and time-resolved studies of the sensitized emission of the excited-state proton tr...
The Human Serum Albumin (HSA) can emit fluorescence (??em=350 nm) under irradiation of ultraviolet l...