ABSTRACT
Especially great successes under investigation of the driving forces of the enzymatic catalysis were achieved in a case of the Chemotrypsin. Chemotrypsin – this is endopeptidase, which cleaves the peptide bonds into peptides. The most important information about the structure of the Chemotrypsin’s molecule has been obtained with the use of the roentgen investigations [1−4]. It was found, that the all charged groups into the molecule of the ferment are directed sideways to the aqueous solution (with the except for the three, which have the special functions into a mechanism action of the active center). The successes in kinetic investigations in the most cases were caused by the works of М. Bergmann, D. Frugonn and H. Neyrag, who determined that the Chemotrypsin can hydrolyze also the simple low−molecular products (amides, esters).
