Journal
ANALYTICAL BIOCHEMISTRY
Volume 334, Issue 2, Pages 297-302Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2004.07.007
Keywords
fullerol; resonance light scattering; proteins; determination
Ask authors/readers for more resources
Fullerol has been synthesized through the reaction of fullerene C-60 with NaOH in aqueous solution by means of ultrasonic agitation and characterized by infrared and H-1-nuclear magnetic resonance spectroscopy. The fullerol obtained shows good solubility and excellent stability in water. A weak resonance light scattering (RLS) spectrum of fullerol was observed in aqueous solution. However, the intensity of the RLS signal could be enhanced in the presence of proteins, including bovine serum albumin (BSA), human serum albumin (HSA), pepsin (Pep), and lysozyme (Lys). Based on the enhancement of the RLS, a sensitive method for the determination of proteins has been established. The quantitative conditions were considered with regard to the effects of the pH, the ion strength, and the concentration of the fullerol. Under the optimum conditions, the intensity of the RLS was proportional to the concentration of proteins with the limits of detection of 9.7, 10.9, 57.4, and 8.5 ng mL(-1) for BSA, HSA, Pep, and Lys, respectively. Almost no interference can be observed from some amino acids, nucleic acids, and most of the metal ions. The model samples and human serum samples were determined satisfactorily with the proposed method. (C) 2004 Elsevier Inc. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available