Chymotrypsinogen A is used as a serine protease that hydrolyzes peptide bonds with aromatic or large hydrophobic side chains (Tyr, Trp, Phe, Met) on the carboxyl end of the peptide bond, used in the non-invasive determination of solid-state protein conformation using near infrared (NIR) spectroscopy. It has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. The enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. In this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution.
Arved Datyner.; Elizabeth Finnimore. A new staining method for the assay of proteins on polyacrylamide gels. Analytical Biochemistry. 1973, 52, (1), 45-55.
Meng, C.K.; Mann, M.; Fenn, J.B. Of protons or proteins. Zeitschrift fur Physik D Atoms, Molecules and Clusters. 1988, 10, (2), 361-368.