Raman spectroscopy of disulfide bridges in thrombin

Abstract

Disulfide bridges of bovine α-thrombin are studied using the analysis of the Raman spectral features in the spectral interval 500–550 cm⁻¹. The changes under study are caused by the transitions from lyophilized state to the native solution in PBS with a protein concentration of 2.8 mM (100 mg/ml) and from native solution to solution with partially reduced disulfide bridges. The reduction takes place when dithiothreitol (DTT) is added to the sample.