Trypsin is an enzyme that can cleave proteins at specific positions. It cuts at R-X and K-X bonds, unless X is P (see amino acids for the codes). Main trypsin preparations contain some chymotrypsin activity. The pH optimum for trypson to work is pH7 - pH9, and it is permanently inactivated at ph>11. Trypsin retains activity in 0.1% SDS, 1 M guanidine HCl and 30% ethanol. The autocatalytic activity of trypsin can be slowed down with 20 mM calcium.
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