title: [Thermodynamics studies on the reaction characteristics of hemoporphyrin with human serum albumin].
abstract: The quenching reaction of hemoporphyrin with human serum albumin (HSA) was studied by using fluorescence spectraand absorption spectra. The formation constants of them were analyzed at different temperature according to Stem-Volmer equation and double-reciprocal equation, which are smaller at high temperature than at low temperature. The binding site was calculated (r = 4.36) by Foster energy transfer mechanism, and the thermodynamic parameters were obtained. H-bond and Van der Waals are two main reactions between HP and HSA.
authors.affiliation: College of Chemistry and Chemical Engineering, Shanxi University, Taiyuan 030006, China.
authors.forename: Yong
authors.initials: Y
authors.lastname: Zhang
authors.forename: Xin-liang
authors.initials: XL
authors.lastname: Yan
authors.forename: Ya-chun
authors.initials: YC
authors.lastname: Lei
authors.forename: Xiao-fang
authors.initials: XF
authors.lastname: Shen
authors.forename: Jing-hao
authors.initials: JH
authors.lastname: Pan
authors.forename: Dian-sheng
authors.initials: DS
authors.lastname: Liu
mesh_terms: D000465:Algorithms; D004735:Energy Transfer; D006415:Hematoporphyrins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D006860:Hydrogen Bonding; D007700:Kinetics; D008956:Models, Chemical; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism; D013050:Spectrometry, Fluorescence; D055672:Static Electricity; D013696:Temperature; D013816:Thermodynamics
chemical_list: D006415:Hematoporphyrins; D012709:Serum Albumin