Microdetermination of proteins using m-carboxychlorophosphonazo as detection probe by enhanced resonance light scattering spectroscopy

Fresenius J Anal Chem. 2000 Dec;368(7):715-9. doi: 10.1007/s002160000563.

Abstract

Proteins can be determined using a common spectrofluorometer to detect the intensity of resonance light scattering (RLS). Under acidic conditions, the reaction between m-carboxychlorophosphonazo (CPA-mK) and proteins enhances the weak light scattering of CPA-mK drastically. This enhanced intensity is proportional to the concentration of proteins. The linear ranges for human serum albumin are 0.5-35.0 microg/mL, with detection limits of 0.104 microg/mL. The method yields results comparable to those of the calorimetric method using Coomassie Brilliant Blue G-250 (CBB) with relative standard deviations of 0.72-2.10% (n = 10). There is almost no interference by amino acids and most of the metal ions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Azo Compounds / chemistry*
  • Calibration
  • Humans
  • Hydrogen-Ion Concentration
  • Indicators and Reagents
  • Light
  • Proteins / analysis*
  • Scattering, Radiation
  • Serum Albumin / chemistry
  • Solutions

Substances

  • Azo Compounds
  • Indicators and Reagents
  • Proteins
  • Serum Albumin
  • Solutions
  • m-carboxychlorophosphonazo