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2. A novel method for determination of protein in human serum utilizing the trihydroxylphenylfluorone-molybdenum(VI) complex as a probe by fluorescence spectrometry.

Author

Wei Q, Hongmin M, Duan C, Wang J, Liu S, and Du B

Subjects
Benzene Derivatives, Blood Proteins isolation & purification, Emulsions, Humans, Hydrogen-Ion Concentration, Indicators and Reagents, Kinetics, Molybdenum, Sensitivity and Specificity, Spectrometry, Fluorescence methods, Blood Proteins analysis
Abstract

The fluorescence intensity of the trihydroxyl-phenylfluorone-molybdenum(VI) [Mo(VI)] complex is quenched by protein. Based on this, a novel method for protein assay in aqueous solution was developed. With pH 3.75 acetic acid-sodium acetate buffer solution, in the presence of p-octyl polyethylene glycol phenyl ether microemulsion, the quenched fluorescence intensity is proportional to the concentration of bovine serum albumin (BSA) in the range of 0-7.00 microg/mL, and the detection limit of BSA is 5.65 ng/mL. There is no interference from amino acids and most metal ions. The method developed in this paper has been used for the successful determination of protein in human serum.

Published
2007

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