General Product Information: Trypsin is isolated from human pancreas and is supplied lyophilized. Protein is determined prior to lyophilization by measuring the absorbance at 280nm (Emg/ml = 1.45). One unit of the enzyme will hydrolyze 1 µmole of N-benzyl-DL-Arg-pNA per minute in 100 mM Tris-HCL, 20mM Calcium Chloride, pH 8.0, at 25°C.
Catalog No. T0614 (Part No. 90250)
Purity: ≥ 95% by SDS-PAGE.
Activity: determined prior to lyophilization.
Sample Certificate, MS Word
Trypsin is an endopeptidase secreted by the pancreas to aid in the
digestion of foods. Because trypsin is highly proteolytic, the pancreas secretes an inactive form of this
enzyme (trypsinogen) into the samll intestine where enterokinase cleaves the N-terminal hexapeptide,
thus activating the enzyme. Trypsin specifically cleaves peptide linkages at the carboxyl group of either
lysine or arginine, and its optimal pH for activity is between pH 8 - 9. Trypsin is most effective on partially
digested proteins. It also digests some proteins, such as protamines and histones, that cannot be digested
by pepsin. The products of trypsin digestion are amono acids and varous polypeptides.
A rare, hereditary trypsinogen deficiency has been reported and results in the significant impairment of
protein digestion. Symptoms include severe growth inhibition, hypoproteinemia, edema, and diarrhea.
Evaluation of pancreatic enzymes in such cases reveals a complete absence of trypsinogen. In addition,
increased serum levels of trypsin are found in individuals with cystic fibrosis.