ICCAS OpenIR
Investigation of the interaction between acridine orange and bovine serum albumin
Feng, XZ; Lin, Z; Yang, LJ; Wang, C; Bai, CL
1998-12-01
Source PublicationTALANTA
ISSN0039-9140
Volume47Issue:5Pages:1223-1229
AbstractThe results from the measurement of the fluorescence spectrum showing the binding characteristics of acridine orange (AO) and bovine serum albumin (BSA) are reported. It was found that the equilibrium constant k = 4848.64 1 mol(-1), and the number of binding sites n = 0.82. Based on the mechanism of the Forster energy transference, the transfer efficiency of energy and distance between the acceptor AO and BSA were found. The interaction between AO and BSA have been verified as consistent with the static quenching procedure and the quenching mechanism is related to the energy transfer. (C) 1998 Elsevier Science B.V. All rights reserved.
KeywordAcridine Orange Bovine Serum Albumin Equilibrium Constant Binding Sites Energy Transfer
Indexed BySCI
Language英语
WOS IDWOS:000077451800018
PublisherELSEVIER SCIENCE BV
Citation statistics
Cited Times:294[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.iccas.ac.cn/handle/121111/74682
Collection中国科学院化学研究所
Corresponding AuthorBai, CL
AffiliationAcad Sinica, Inst Chem, Beijing 100080, Peoples R China
Recommended Citation
GB/T 7714
Feng, XZ,Lin, Z,Yang, LJ,et al. Investigation of the interaction between acridine orange and bovine serum albumin[J]. TALANTA,1998,47(5):1223-1229.
APA Feng, XZ,Lin, Z,Yang, LJ,Wang, C,&Bai, CL.(1998).Investigation of the interaction between acridine orange and bovine serum albumin.TALANTA,47(5),1223-1229.
MLA Feng, XZ,et al."Investigation of the interaction between acridine orange and bovine serum albumin".TALANTA 47.5(1998):1223-1229.
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