[Thermodynamics studies on the reaction characteristics of hemoporphyrin with human serum albumin].
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.
Zhang
Yong
Y
College of Chemistry and Chemical Engineering, Shanxi University, Taiyuan 030006, China.
Yan
Xin-liang
XL
Lei
Ya-chun
YC
Shen
Xiao-fang
XF
Pan
Jing-hao
JH
Liu
Dian-sheng
DS
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
D006415:Hematoporphyrins; D012709:Serum Albumin