Journal ArticleDOI
Methyl parathion interaction with human and bovine serum albumin
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TLDR
Results suggest that the primary binding site for methyl parathion on albumin is close to tryptophan residues 214 of human serum albumin and 212 of bovine serum albumIn, and suggest that this pesticide is potentially toxic for both vertebrates and invertebrates.About:
This article is published in Toxicology Letters.The article was published on 2004-02-28. It has received 204 citations till now. The article focuses on the topics: Bovine serum albumin & Serum albumin.read more
Citations
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Study of the interaction of an anticancer drug with human and bovine serum albumin: Spectroscopic approach
TL;DR: Experimental results showed that the binding of GEM to BSA or HSA induced conformational changes in BSA and HSA, and confirmed that the secondary structure of protein was altered by GEM.
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Binding of serum albumins with bioactive substances – Nanoparticles to drugs
TL;DR: In this paper, the interaction of various nanomaterials, antibiotics, anticancer drugs, anti-inflammatory agents, dyes, flavonoids, and certain noxious materials with serum albumin is discussed.
Journal ArticleDOI
Studies of the interaction between paraquat and bovine hemoglobin.
Yanqing Wang,Hongmei Zhang,Gen-Cheng Zhang,Shuang-Xia Liu,Qiu-Hua Zhou,Zhenghao Fei,Zong-Tang Liu +6 more
TL;DR: Hydrophobic and electrostatic interactions played a major role in stabilizing the complex and fluorescence quenching of BHb by PQ was a result of the formation of PQ-BHb complex.
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Synthesis, characterization and interaction studies of copper based drug with Human Serum Albumin (HSA): spectroscopic and molecular docking investigations.
TL;DR: The results of fluorescence titration revealed that the complex 1 strongly quench the intrinsic fluorescence of HSA through a static quenching procedure, revealing that the hydrophobic and hydrogen bonding interactions play a major role in HSA-complex 1 association.
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Studies on the interaction between imidacloprid and human serum albumin: spectroscopic approach.
TL;DR: The experimental results showed that the fluorescence quenching of HSA by IMI was a result of the formation of IMI-HSA complex; staticQuenching was confirmed to result in the fluorescent quenched.
References
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Book
Principles of fluorescence spectroscopy
TL;DR: This book describes the fundamental aspects of fluorescence, the biochemical applications of this methodology, and the instrumentation used in fluorescence spectroscopy.
Journal ArticleDOI
Atomic structure and chemistry of human serum albumin.
Xiao Min He,Daniel C. Carter +1 more
TL;DR: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 Å and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serumalbumin.
Book
All About Albumin: Biochemistry, Genetics, and Medical Applications
TL;DR: The Albumin Molecule: Its Structure and Chemical Properties and Practical Aspects: Albumin in the Laboratory.
Journal ArticleDOI
Crystal structure of human serum albumin at 2.5 A resolution.
TL;DR: A new triclinic crystal form of human serum albumin (HSA), derived either from pool plasma or from a Pichia pastoris expression system, was obtained from polyethylene glycol 4000 solution, and three-dimensional structures of pHSA and rHSA were determined.
Related Papers (5)
Thermodynamics of protein association reactions: forces contributing to stability
Philip D. Ross,S. Subramanian +1 more