On the factors affecting the enhanced resonance light scattering signals of the interactions between proteins and multiply negatively charged chromophores using water blue as an example
On the factors affecting the enhanced resonance light scattering signals of the interactions between proteins and multiply negatively charged chromophores using water blue as an example
Engineering Village 2
2006 Elsevier Inc.
Accession number: 06029636813
Title: On the factors affecting the enhanced resonance light scattering signals of the interactions between proteins and multiply negatively charged chromophores using water blue as an example
Authors: Huang, Cheng Zhi; Lu, Wei; Li, Yuan Fang; Huang, Yu Ming
Author affiliation: College of Chemistry and Chemical Engineering, Southwest University, Chongqing 400715, China
Serial title: Analytica Chimica Acta
Abbreviated serial title: Anal. Chim. Acta
Volume: v 556
Issue: n 2
Issue date: Jan 25 2006
Publication year: 2006
Pages: p 469-475
Language: English
ISSN: 0003-2670
CODEN: ACACAM
Document type: Journal article (JA)
Publisher: Elsevier, Amsterdam, 1000 AE, Netherlands
Abstract: Electrostatic interactions of proteins, including bovine serum albumin (BSA), human serum albumin (HSA), ?-globulin (?-IgG), a-chymotrypsin (Chy), lysozyme (Lys) and cellulase (Cel), with multiply negatively charged chromophores were investigated based on the measurements of the enhanced resonance light scattering (RLS) signals. Using triply negatively charged water blue (WB) as an example, the factors were discussed that affect the enhanced resonance light scattering signals of the interactions between proteins and the negatively charged chromophores. It was found that the enhanced RLS signals with the maximum light scattering peak at 346.0 nm in these interacting systems are strongly dependent on the isoelectric points of proteins and show adverse linear relationships with increasing ionic strength depending on the positive charges of the inorganic metal ions used to control the ionic strength of the medium, sufficiently disclosing that the electrostatic attraction performs an important role in the combination of proteins with WB. Linear responses were discovered between the enhanced RLS signals and the protein molecular weights (Mw), displaying the dimensions of scattered particles formed by proteins and WB make a key contribution to the RLS enhancements. An empirical equation is proposed which possibly displays the factors affecting the enhanced RLS signals of the interactions between proteins with negatively charged chromophores. ? 2005 Elsevier B.V. All rights reserved.
Number of references: 25
Ei main heading: Proteins
Ei controlled terms: Chromophores - Light scattering - Signal processing - Water - Electrostatics - Enzymes
Uncontrolled terms: Electrostatic interactions - Water blue - Human serum albumin (HSA)
Ei classification codes: 804.1 Organic Compounds - 741.1 Light/Optics - 716.1 Information & Communication Theory - 804.2 Inorganic Compounds - 701.1 Electricity: Basic Concepts & Phenomena - 461.2 Biological Materials
Treatment: Theoretical (THR); Experimental (EXP)
DOI: 10.1016/j.aca.2005.09.048
Database: Compendex
Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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