title: Study on the multiple sites binding of human serum albumin and porphyrin by affinity capillary electrophoresis.
abstract: Equations to describe the two sites binding between proteins and ligands were deduced. According to these equations, not only the binding constants, but also the mole fraction of proteins in different forms could be obtained. Using the published data on the interaction between human serum albumin (HSA) and three kinds of porphyrin (coproporphyrin (CP), uroporphyrin I (UP) and protoporphyrin (PP)), a further study on their binding was carried out. It was concluded that there may exist two binding sites with the binding constants at the first site, proved to be the preferential one, being 6.50 x l0(5), 1.94 x 10(6) and 8.94 x 10(5), respectively. In addition, it was also demonstrated that the two binding sites of HSA with CP and UP might be of different kinds, though those of HSA and PP were of the same kind but at different positions.
authors.affiliation: National Chromatographic R&A Center, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, PR China.
authors.forename: Weibing
authors.initials: W
authors.lastname: Zhang
authors.forename: Lihua
authors.initials: L
authors.lastname: Zhang
authors.forename: Guichen
authors.initials: G
authors.lastname: Ping
authors.forename: Yukui
authors.initials: Y
authors.lastname: Zhang
authors.forename: A
authors.initials: A
authors.lastname: Kettrup
mesh_terms: D001665:Binding Sites; D019075:Electrophoresis, Capillary / Q000379:methods*; D006801:Humans; D011166:Porphyrins / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism*
chemical_list: D011166:Porphyrins; D012709:Serum Albumin