Binding studies of three water-soluble polycationic porphyrins with human serum albumin.
The binding stoichiometry and equilibria of three polycationic water-soluble porphyrins with human serum albumin (HSA) have been determined by fluorescence quenching and filtration methods in 0.1M phosphate buffer, pH 7.2 at 25 degrees. For one porphyrin the binding equilibrium was also measured by measuring the lifetime of tryptophan and also by measuring the polarization of bound porphyrin. Energy transfer between the porphyrin and the tryptophan residue of HSA has been studied.
Datta-Gupta
N
N
Department of Natural Sciences, South Carolina State College, Orangeburg 29117.
Malakar
D
D
Walters
E
E
Thompson
B
B
D006801:Humans; D011166:Porphyrins / Q000378:metabolism*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D011166:Porphyrins; D012709:Serum Albumin; C021096:tetra(4-N-methylpyridyl)porphine; C057456:tetra(2-N-methylpyridyl)porphine; C057459:tetra(3-N-methylpyridyl)porphine