Binding studies of four free base porphyrins and six iron (+3) porphyrins with human serum albumin.
The binding stoichiometry and binding equilibria of human serum albumin with water-soluble four free base porphyrins and six chloroiron (+3) porphyrins have been determined in 0.1M phosphate buffer, pH 7.2, by fluorescence quenching and filtration methods. The binding stoichiometry is observed to be 1:1, porphyrin to protein. The dissociation constants, Kd, between the porphyrins and the protein are found to be 1-4 microM. A binding mechanism between the protein and the porphyrins has been presented.
Datta-Gupta
N
N
Department of Natural Sciences, South Carolina State College, Orangeburg 29117.
Malakar
D
D
Dozier
J
J
D006801:Humans; D007501:Iron / Q000097:blood*; D011166:Porphyrins / Q000097:blood*; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D014462:Ultrafiltration
D011166:Porphyrins; D012709:Serum Albumin; D007501:Iron