Effects of the Interaction of Rifamycin SV with Serum Albumins on the Resonance Rayleigh Scattering Spectra and Their Analytical Application

• Published in: Chinese journal of chemistry Vol. 26; no. 5; pp. 893 - 897
• Main Authors: YANG, Ji-Dong, CAO, Tuan-Wu, LIU, Zhong-Fang, KONG, Ling, LIU, Shao-Pu
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 01.05.2008; WILEY‐VCH Verlag; Wiley Subscription Services, Inc
• Subjects: protein determination; resonance rayleigh scattering (RRS); rifamycin SV (RFSV); serum albumin
• ISSN: 1001-604X; 1614-7065
• DOI: 10.1002/cjoc.200890164

In pH 4.5–4.8 Britton‐Robinson buffer solution, rifamycin SV (i.e. rifamycin sodium) can react with serum albumin such as human serum albumin (HSA) and bovine serum albumin (BSA) to form macromolecular complexes by electrostatic attraction and hydrophobic force. As a result, the resonance Rayleigh scattering (RRS) of the drug was enhanced remarkably and the RRS peaks were at 374 and 552 nm. The enhancement of RRS (ΔI) is directly proportional to the concentration of HSA or BSA. The linear ranges and the detection limits are 0.03–6.0 µg/mL and 9.0 ng/mL for HSA, and 0.01–8.0 µg/mL and 2.0 ng/mL for BSA, respectively. In this work, a sensitive, selective, simple and fast method for the determination of trace amounts of serum albumin by RRS technique has been developed, which was applied to the determination of serum albumin in the synthesized samples and human urine samples with satisfactory results.