Determination of proteins at nanogram levels based on their enhancement effects of Rayleigh light scattering on dibromomethylchlorophosphonazo

Spectrochim Acta A Mol Biomol Spectrosc. 2000 Nov 1;56A(12):2465-70. doi: 10.1016/s1386-1425(00)00329-2.

Abstract

A new Rayleigh light scattering (RLS) assay of protein was conducted in this paper. At the optimum pH conditions, and in the presence of Tween-20, the weak RLS of dibromomethylchlorophosphonazo (DBM-CPA) can be enhanced greatly by the addition of proteins. Based on this, the reactions of DBM-CPA and proteins were studied. A new quantitative determination method for proteins has been developed. The method is simple, practical and relatively free from interference from coexisting substances, as well as much more sensitive (the dynamic ranges of 0.065-40.05 microg ml(-1) and detection limit of 30 ng ml(-1) for bovine serum albumin (BSA)) than most of the existing assays. The determination results of human body serum samples are identical to those by the CBB method, with relative S.D. of six determination of 0.5-2.2%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blood Proteins / analysis
  • Calibration
  • Humans
  • Light
  • Organophosphorus Compounds / chemistry*
  • Proteins / analysis*
  • Scattering, Radiation*
  • Sensitivity and Specificity
  • Serum Albumin, Bovine / analysis
  • Solutions
  • Surface-Active Agents / chemistry

Substances

  • Blood Proteins
  • Organophosphorus Compounds
  • Proteins
  • Solutions
  • Surface-Active Agents
  • Serum Albumin, Bovine