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Microdetermination of Proteins by Enhanced Rayleigh Light Scattering Spectroscopy with Thorin 被引量:2

Microdetermination of Proteins by Enhanced Rayleigh Light Scattering Spectroscopy with Thorin
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摘要 In acidic solution, thorin (2-(2-hydroxy-3.6-disulfo-1-naph-thyl)-azo-phenylarsenic acid sodium salt) can be bound with proteinand aggregated to form large particle which displays a very strong rayleigh light scattering (RLS).The effects of pH, thorin concentration, detergent and ionic strength on binding reaction have beenstudied. The interference of coexisting substances was checked. The Scatchard plots for reactionbetween thorin and bovine serum albumin (BSA) were constructed and the association constant ofthorin-BSA was obtained, it is 5.26 x 10~5 L/mol, the maximum binding number is 7. RLS intensity iswell proportional to the concentrations of 2.0―14.0 μg/ mL for human serum albumin (HSA),1.8―14.7 μg/mL for BSA and 1.8―14.6 μg/mL for γ-globulin (γ-G). The detection limits (3σ) are54.1 ng/mL for HSA, 52.0 ng/mL for BSA and 51.8 ng/mL for γ-G, respectively. The relative standarddeviation is 2.4% for BSA, 3.2% for HSA and 4.1% for γ-G. The human serum samples were measuredsatisfactorily by using this method. In acidic solution, thorin (2-(2-hydroxy-3.6-disulfo-1-naph-thyl)-azo-phenylarsenic acid sodium salt) can be bound with proteinand aggregated to form large particle which displays a very strong rayleigh light scattering (RLS).The effects of pH, thorin concentration, detergent and ionic strength on binding reaction have beenstudied. The interference of coexisting substances was checked. The Scatchard plots for reactionbetween thorin and bovine serum albumin (BSA) were constructed and the association constant ofthorin-BSA was obtained, it is 5.26 x 10~5 L/mol, the maximum binding number is 7. RLS intensity iswell proportional to the concentrations of 2.0―14.0 μg/ mL for human serum albumin (HSA),1.8―14.7 μg/mL for BSA and 1.8―14.6 μg/mL for γ-globulin (γ-G). The detection limits (3σ) are54.1 ng/mL for HSA, 52.0 ng/mL for BSA and 51.8 ng/mL for γ-G, respectively. The relative standarddeviation is 2.4% for BSA, 3.2% for HSA and 4.1% for γ-G. The human serum samples were measuredsatisfactorily by using this method.
机构地区 DepartmentofChemistry
出处 《Chinese Journal of Chemistry》 SCIE CAS CSCD 2002年第4期368-373,共6页 中国化学(英文版)
基金 theNationalNaturalScienceFoundationofChina (No.2 9775 0 0 3)
关键词 thorin PROTEIN rayleigh light scattering thorin protein rayleigh light scattering
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参考文献6

  • 1Ya-Ting Wang,Feng-Lin Zhao,Ke-An Li,Shen-Yang Tong.Microdetermination of proteins by enhanced Rayleigh light scattering spectroscopy with morin[J].Fresenius’ Journal of Analytical Chemistry.1999(6)
  • 2Wetlaufer,D. B. Advances in Protein Chemistry . 1962
  • 3Kirschenbaum,D. M. Analytical Biochemistry . 1973
  • 4Scatchard,G. Annals of the New York Academy of Sciences . 1949
  • 5Bradford,M. M. Analytical Biochemistry . 1976
  • 6Julio,C.Paula, D; Pobblee, J.H. ; Pasternack, R. F[].Biophysical Journal.1995

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