Abstrato

Stability of bovine serum albumin labelled by rhodamine B isothiocyanate

Ting Yang, Dali Sun, Pengyuan Xu, Shumin Li, Yunyun Cen, Yijun Li, Qinwen Xu, Yanbo Sun, Weiming Li, Yueying Lin, Yuxing Qi, Xiongzhi Chen

The aim of this study was to label Bovine Serum Albumin (BSA) by Rhodamine B Isothiocyanate (RBITC) and test its stability in vivo. RBITC-BSA was labelled by the improved Marshall’s method, scanned at full wavelength, and the RBITC:BSA ratio was calculated. Blood and urine samples were obtained from rabbits injected with the RBITC-BSA complex and SDS-PAGE analysis was performed. Full wavelength scanning showed that the labelled RBITC-BSA complex possessed features of both RBITC and BSA, and the RBITC:BSA ratio was 1:80. Furthermore, the RBITC-BSA complex was stable in vivo. Thus, we developed a stable RBITC-BSA complex with high specificity and sensitivity, which could be used as a tracer molecule to study protein transportation and vascular permeability.