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Trypsin (porcine pancreas)

Cat. No. M10184
Trypsin (porcine pancreas) Structure
Size Price Availability Quantity
10g USD 42  USD42 In stock
25g USD 84  USD84 In stock
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Quality Control & Documentation
Biological Activity

Trypsin is a serine protease in the digestive system of human and animals. The main function of this enzyme is to hydrolyze proteins into smaller peptides or even amino acids. Trypsin cleaves peptides on the C-terminal side of lysine and arginine residues. The rate of hydrolysis of this reaction is slowed if an acidic residue is on either side of the cleavage site and hydrolysis is stopped if a proline residue is on the carboxyl side of the cleavage site. The optimal pH for trypsin activity is 7-9. Trypsin can also act to cleave ester and amide linkages of synthetic derivatives of amino acids. EDTA is added to trypsin solutions as a chelating agent that neutralizes calcium and magnesium ions that obscure the peptide bonds on which trypsin acts. Removing these ions increases the enzymatic activity.

Product Citations
Chemical Information
Molecular Weight 725.78
Formula C35H47N7O10
CAS Number 9002-07-7
Solubility (25°C) Soluble in water (10 mg/ml)
Soluble in phosphate buffers (10 mg/ml)
Storage 2-8°C, dry, sealed
Conversion of different model animals based on BSA (PMID: 27057123)
Species Mouse Rat Rabbit Guinea pig Hamster Dog
Weight (kg) 0.02 0.15 1.8 0.4 0.08 10
Body Surface Area (m2) 0.007 0.025 0.15 0.05 0.02 0.5
Km factor 3 6 12 8 5 20
Animal A (mg/kg) = Animal B (mg/kg) multiplied by  Animal B Km
Animal A Km

For example, to modify the dose of Compound A used for a mouse (20 mg/kg) to a dose based on the BSA for a rat, multiply 20 mg/kg by the Km factor for a mouse and then divide by the Km factor for a rat. This calculation results in a rat equivalent dose for Compound A of 10 mg/kg.

References

[1] Norelle L Daly, et al. J Biol Chem. Structural insights into the role of the cyclic backbone in a squash trypsin inhibitor

[2] Paul P Geurink, et al. J Med Chem. Incorporation of non-natural amino acids improves cell permeability and potency of specific inhibitors of proteasome trypsin-like sites

[3] Masayuki Shimoda, et al. Cell Transplant. Improvement of porcine islet isolation by inhibition of trypsin activity during pancreas preservation and digestion using α1-antitrypsin

[4] R J Read, et al. Biochemistry. Critical evaluation of comparative model building of Streptomyces griseus trypsin

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