NDLI: Spectroscopic Investigation on the Toxicological Interactions of 4-aminoantipyrine with Bovine Hemoglobin

Content Provider	Springer Nature Link
Author	Teng, Yue Liu, Rutao Yan, Shifeng Pan, Xingren Zhang, Pengjun Wang, Meijie
Copyright Year	2009
Abstract	The effects of 4-aminoantipyrine (AAP) on bovine hemoglobin (BHb) were investigated by fluorescence spectroscopy, synchronous fluorescence spectroscopy, ultraviolet-visible absorption spectroscopy and circular dichroism spectroscopy (CD) under simulated physiological conditions. The experimental results showed that AAP effectively quenched the intrinsic fluorescence of BHb via static quenching. The number of binding sites, the binding constant K$_{a}$, and the thermodynamic parameters (ΔH$^{○}$, ΔS$^{○}$ and ΔG$^{○}$) were measured at two different temperatures. Van der Waals’ interactions and hydrogen bonds were the predominant intermolecular forces in stabilizing the BHb-AAP complex. The experiment results confirmed micro-environmental and conformational changes of BHb in the presence of AAP. The α-helix content decreased, indicating that AAP destroys some of the hydrogen bonding networks in the polypeptide chain.
Starting Page	381
Ending Page	387
Page Count	7
File Format	PDF
ISSN	10530509
Journal	Journal of Fluorescence
Volume Number	20
Issue Number	1
e-ISSN	15734994
Language	English
Publisher	Springer US
Publisher Date	2009-09-29
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	4-aminoantipyrine Bovine hemoglobin Multi-spectroscopic techniques Toxicity evaluation Analytical Chemistry Biochemistry Biotechnology Biophysics and Biological Physics Biomedicine general
Content Type	Text
Resource Type	Article
Subject	Sociology and Political Science Spectroscopy Law Biochemistry Clinical Biochemistry Clinical Psychology

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