| Citation | Distinguished for his studies on the structure and mode of action of the proteolytic enzymes. In particular, he has determined the complete amino acid sequence of chymotrypsinogen, a protein of 253 residues, and has studied the relationship of this structure to enzymic activity. He has developed two important new techniques in protein chemistry: the "dansyl" methods for determining sequences in peptides on a very small scale, and the "diagonal" technique for studying the distribution of disulphide bridges in proteins. His comparative studies on other pancreatic proteolytic enzymes have revealed interesting homologies, which give information about the biological origin of the proteins and their mode of action.
His earlier kinetic studies on chymotrypsin demonstrated the formation of an acyl enzyme as an intermediate in the hydrolysis reaction. |