Soluble in water; practically insoluble in alcohol and glycerol.
One USP trypsin unit is the activity causing a change in absorbance of 0.003 per minute under the conditions specified.
The protease activity of trypsin is highly specific toward positively charged side chains with lysine and arginine. Forms complexes with a2-macroglobulin.Can be used in the isolation of intact, detergent-free phycobilisomesand in the hydrolysis/condensation of carboxylic ester bonds.
Inhibitors: Trypsin is inhibited by organophosphorus compounds such as diisopropyl fluorophosphate and natural trypsin inhibitors from pancreas, soybean, lima bean and egg white. Silver ions are also potent inhibitors. Specific inhibitors are AEBSF, antipain, aprotinin, DFP, leupeptin, PMSF, TLCK, and Trypsin Inhibitor. Solutions: Solutions of trypsin should be thawed and swirled gently to mix. Solutions are relatively stable for periods of up to three months under refrigeration. If longer storage is desired, the concentrate should be aliquoted and refrozen. Thawed concentrate may contain a small amount of precipitate; this is normal and in no way will affect the efficacy of the product.
Trypsin is used to re-suspend cells adherent to the cell culture dish wall during the process of harvesting cells. Trypsin can also be used to dissociate dissected cells. Trypsin can be used to break down casein in breast milk. Trypsin is commonly used in biological research during proteomics experiments to digest proteins into peptides for mass spectrometry analysis. Trypsin can also be used to dissolve blood clots in its microbial form and treat inflammation in its pancreatic form.
