Fluorimetric determination of proteins using 4-chloro-(2′-hydroxylophenylazo)rhodanine–Ti(IV) complex as a spectral probe
Article first published online: 4 JUN 2008
Copyright © 2008 John Wiley & Sons, Ltd.
Volume 23, Issue 5, pages 333–337, October 2008
How to Cite
Sun, S., Ma, H., Chen, X., Zhang, N., Wu, D., Du, B. and Wei, Q. (2008), Fluorimetric determination of proteins using 4-chloro-(2′-hydroxylophenylazo)rhodanine–Ti(IV) complex as a spectral probe. Luminescence, 23: 333–337. doi: 10.1002/bio.1041
- Issue published online: 17 SEP 2008
- Article first published online: 4 JUN 2008
- Manuscript Accepted: 28 JAN 2008
- Manuscript Revised: 24 JAN 2008
- Manuscript Received: 28 AUG 2007
- spectral probe;
A novel method for the determination of proteins was developed, based on the enhancement of fluorescence with 4-chloro-(2′-hydroxylophenylazo)rhodanine–Ti(IV) [ClHARP–Ti(IV)] complex as a fluorescence probe. The excitation and emission wavelengths of the system were 335 nm and 376 nm, respectively. The presence of bis(2-ethylhexyl)sulphosuccinate sodium salt (AOT) microemulsion greatly increased the sensitivity of the system. Under optimal conditions, four kinds of proteins, including bovine serum albumin (BSA), human serum albumin (HSA), egg albumin (Ova), and γ-globin (γ-G) were studied. The detection limits were 0.182 µg/mL for BSA, 0.0788 µg/mL for HSA, 0.216 µg/mL for Ova and 0.484 µg/mL for γ-G. The linear ranges of the calibration were 0–12.0, 0–10.0, 0–18.0 and 0–18.0 µg/mL, respectively. The method possessed high sensitivity, good selectivity and was applied to the analysis of protein in milk powder and cornmeal with satisfactory results. Copyright © 2008 John Wiley & Sons, Ltd.