Interaction of triprolidine hydrochloride with serum albumins: Thermodynamic and binding characteristics, and influence of site probes

Journal of Pharmaceutical and Biomedical Analysis

Volumn 54, Issue 5, 2011, Pages 1180-1186

  Sandhya, B ^a   Hegde, Ashwini H ^a   Kalanur, Shankara S ^a   Katrahalli, Umesha ^a   Seetharamappa, J ^a  

^a KARNATAK UNIVERSITY   (India)

Author keywords

Fluorescence quenching; Serum albumins; Spectroscopic methods; Thermodynamic parameters; Triprolidine hydrochloride

Indexed keywords

BOVINE SERUM ALBUMIN; CALCIUM; COBALT; CUPRIC ION; HUMAN SERUM ALBUMIN; MANGANESE; NICKEL; POTASSIUM; TRIPROLIDINE; ZINC;

ARTICLE; BINDING AFFINITY; BINDING SITE; CIRCULAR DICHROISM; DRUG PROTEIN BINDING; FLUORESCENCE RESONANCE ENERGY TRANSFER; FLUORESCENCE SPECTROSCOPY; FORCE; HYDROGEN BOND; INFRARED SPECTROSCOPY; PRIORITY JOURNAL; THERMODYNAMICS;

ANIMALS; BINDING SITES; CATTLE; CIRCULAR DICHROISM; ENERGY TRANSFER; HISTAMINE H1 ANTAGONISTS; HUMANS; HYDROGEN BONDING; MODELS, CHEMICAL; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SERUM ALBUMIN; SERUM ALBUMIN, BOVINE; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS; TRIPROLIDINE;

EID: 78751702234     PISSN: 07317085     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jpba.2010.12.012     Document Type: Article

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