Source: Bovine Pancreas
I.U.B.: 3.4.21.4
Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Worthington Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.
Uses: For tissue culture work, Worthington trypsin, Codes: TRL, TRLS, TRLVMF and TRTVMF have been used by many researchers.
Stability/Storage: Most grades of Worthington trypsin are stable for 2-3 years when stored at 2-8°C. Protect from moisture.
Unit Definitions: TAME Unit: One Unit hydrolyzes 1 µmole of p-toluene-sulfonyl-L-arginine methyl ester (TAME) per minute at 25°C, pH 8.2, in the presence of 10 mM calcium.
Note: 1mg trypsin ≥180 TAME units, 10,350 BAEE units, 3,450 USP/NF units.
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