STRUCTURE IDENTIFICATION AND AFFINITY CHARACTERIZATION OF SOYBEAN AGGLUTININ- CARBOHYDRATE INTERACTION EPITOPES USING PROTEOLYTIC AFFINITY- MASS SPECTROMETRY (PROTEX-MS)

STRUCTURE IDENTIFICATION AND AFFINITY CHARACTERIZATION OF SOYBEAN AGGLUTININ- CARBOHYDRATE INTERACTION EPITOPES USING PROTEOLYTIC AFFINITY- MASS SPECTROMETRY (PROTEX-MS)

We recently reported a new affinity-mass spectrometry-based approach that employs selective proteolytic digestion of the lectin to identify the carbohydrate binding sites. However, lectins such as Soybean Agglutinin (SBA) are resistant to enzyme hydrolysis and require time-consuming proteolytic digestion procedures to be inactivated. 

Here, we show the application of pressure-enhanced proteolytic digestion for fast and effective enzyme hydrolysis together with an affinity-mass spectrometry-based approach for the molecular identification of carbohydrate recognition structures, with high specificity, sensitivity and low requirements of sample purity.