作者: Nicholas R. Harn , Yunhua N. Jeng , James G. Kostelc , C.Russell Middaugh
DOI: 10.1002/JPS.20464
关键词:
摘要: ABSTRACT: Spectroscopy was employed to analyze the structural and thermal stability of highly concentrated oil suspensions bovine somatotropin (bST). These methods were then compared with more dilute aqueous solutions (1 10 mg/mL). All opaque, viscous, in bST (>300 mg/mL) thus provided unique analytical challenges. Using front surface fluorescence ATR-FTIR spectroscopy, protein structure could be directly monitored this environment. Differences detected between formulations. Fluorescence spectroscopy found that thermally stabile within suspensions, since minimal changes emission peak maxima intensity observed increasing temperature when solutions. It also amount aggregate a sample had some effect on spectra. As aggregated increased, maximum changed. Employing ATR-FTIR, secondary examined temperature. The very no change relative helix/random is up 70°C while significant losses are solution. This study demonstrates conformational can analyzed concentrated, opaque environments using slight modifications conventional methods.