Spectrophotometric study on the interaction between proteins and chlorosulfophenol M and its analytical application
HU Qiu-luan
Abstract
HU Qiu-luan
Abstract
Chlorosulfophenol M is a colouring reagent for the determination of some inorganic ions.It was found that chlorosulfophenol M could bind with serum proteins to form complex in Britton-Robinson buffer at pH 4.23,which presents a maximum absorption at 615nm with 63nm of red shift compared to chlorosulfophenol M itself.A molar absorptivity of 4.34×10~5L·mol~(-1)·cm~(-1)(BSA) and linear range of 0~100mg/L for protein were determined.This method has been used for the determination of the total protein in human serum samples.The results obtained by this method agreed well with those obtained by coomassie brilliant blue G-250 method.Furthermore,the performance and reproducibility are superior to coomassie brilliant blue G-250 method.
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Chlorosulfophenol M is a colouring reagent for the determination of some inorganic ions.It was found that chlorosulfophenol M could bind with serum proteins to form complex in Britton-Robinson buffer at pH 4.23,which presents a maximum absorption at 615nm with 63nm of red shift compared to chlorosulfophenol M itself.A molar absorptivity of 4.34×10~5L·mol~(-1)·cm~(-1)(BSA) and linear range of 0~100mg/L for protein were determined.This method has been used for the determination of the total protein in human serum samples.The results obtained by this method agreed well with those obtained by coomassie brilliant blue G-250 method.Furthermore,the performance and reproducibility are superior to coomassie brilliant blue G-250 method.
Key concepts: Coomassie Brilliant Blue, Chemistry, Molar absorptivity, Reagent, Chromatography, Bradford protein assay, Phosphate buffered saline, Buffer solution