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Determination of proteins at nanogram levels based on their resonance light scattering decrease effect on the dibromo-o- nitrophenylfluorone-sodium lauroyl glutamate system
A novel method for the determination of proteins at nanogram levels was proposed based on the decrease of resonance light scattering (RLS) signal resulting from the interaction of dibromo-o-nitrophenylfluorone (DBONPF)-sodium lauroyl glutamate (SLG) with proteins. At pH 2.97, the decrease RLS intens...
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Published in: | Mikrochimica acta (1966) 2006-02, Vol.153 (1-2), p.65-71 |
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container_end_page | 71 |
container_issue | 1-2 |
container_start_page | 65 |
container_title | Mikrochimica acta (1966) |
container_volume | 153 |
creator | Chen, Zhanguang Zhang, Taiyu Ren, Fenglian Ding, Weifeng |
description | A novel method for the determination of proteins at nanogram levels was proposed based on the decrease of resonance light scattering (RLS) signal resulting from the interaction of dibromo-o-nitrophenylfluorone (DBONPF)-sodium lauroyl glutamate (SLG) with proteins. At pH 2.97, the decrease RLS intensity was proportional to the concentration of proteins in the range of nanogram levels with 3sigma detection limits being 3.4ngmL for bovine serum albumin (BSA), 1.7ngmL for human serum albumin (HSA), 4.1ngmL for gamma-globulin (gamma-IgG), 4.4ngmL for egg albumin, 6.2ngmL for pepsin (Pep) and 3.7ngmL for alpha-chymotrypsin (Chy). The method is no protein-to-protein variability, simple, rapid, practical and relatively free from interference from coexisting substance, as well as much more sensitive than most of the reported methods. The proposed method was successfully applied to determine total protein in human serum samples. |
doi_str_mv | 10.1007/s00604-005-0425-5 |
format | article |
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At pH 2.97, the decrease RLS intensity was proportional to the concentration of proteins in the range of nanogram levels with 3sigma detection limits being 3.4ngmL for bovine serum albumin (BSA), 1.7ngmL for human serum albumin (HSA), 4.1ngmL for gamma-globulin (gamma-IgG), 4.4ngmL for egg albumin, 6.2ngmL for pepsin (Pep) and 3.7ngmL for alpha-chymotrypsin (Chy). The method is no protein-to-protein variability, simple, rapid, practical and relatively free from interference from coexisting substance, as well as much more sensitive than most of the reported methods. 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At pH 2.97, the decrease RLS intensity was proportional to the concentration of proteins in the range of nanogram levels with 3sigma detection limits being 3.4ngmL for bovine serum albumin (BSA), 1.7ngmL for human serum albumin (HSA), 4.1ngmL for gamma-globulin (gamma-IgG), 4.4ngmL for egg albumin, 6.2ngmL for pepsin (Pep) and 3.7ngmL for alpha-chymotrypsin (Chy). The method is no protein-to-protein variability, simple, rapid, practical and relatively free from interference from coexisting substance, as well as much more sensitive than most of the reported methods. 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source | Springer Nature |
subjects | Analytical chemistry Chemistry Exact sciences and technology Spectrometric and optical methods |
title | Determination of proteins at nanogram levels based on their resonance light scattering decrease effect on the dibromo-o- nitrophenylfluorone-sodium lauroyl glutamate system |
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