Trypsin Chymotrypsin Mix
The time tested anti -inflammatory

Trypsin Chymotrypsin Mix is a unique anti - inflammatory product manufactured by Advanced Enzyme Technologies.

Trypsin Chymotrypsin Mix is a proteolytic enzyme obtained by controlled proteolysis of zymogens form in the frozen glands. Successive conc. and purification steps give Trypsin Chymotrypsin Mix best suitable for pharmaceutical applications.

Trypsin and chymotrypsin, like most proleotytic enzymes, are synthesized as inactive zymogen precursors (trypsinogen and chymotrypsinogen) to prevent unwanted destruction of cellular proteins, and to regulate when and where enzyme activity occurs. The inactive zymogens are secreted into the duodenum, where they travel the small and large intestines prior to excretion. Zymogens also enter the bloodstream, where they can be detected in serum prior to excretion in urine. Zymogens are converted to the mature, active enzyme by proteolysis to split off a pro-peptide, either in a subcellular compartment or in an extracellular space where they are required for digestion.

Trypsin and chymotrypsin are structurally very similar, although they recognise different substrates. Trypsin acts on lysine and arginine residues, while chymotrypsin acts on large hydrophobic residues such as tryptophan, tyrosine and phenylalanine, both with extraordinary catalytic efficiency. Both enzymes have a catalytic triad of serine, histidine and aspartate within the S1 binding pocket, although the hydrophobic nature of this pocket varies between the two, as do other structural interactions beyond the S1 pocket.

The human pancreas secretes three isoforms of trypsinogen: cationic (trypsinogen-1), anionic (trypsinogen-2) and mesotrypsinogen (trypsinogen-3). Cationic and anionic trypsins are the major isoforms responsible for digestive protein degradation, occurring in a ratio of 2:1, while mesotrypsinogen accounts for less than 5% of pancreatic secretions. Mesotrypsin is a specialised protease known for its resistance to trypsin inhibitors. It is thought to play a special role in the degradation of trypsin inhibitors, possibly to aid in the digestion of inhibitor-rich foods such as soybeans and lima beans. An alternatively spliced mesotrypsinogen in which the signal peptide is replaced with a different exon 1 is expressed in the human brain; the function of this brain trypsinogen is unknown.

There are two isoforms of pancreatic chymotrypsin, A and B, which are known to cleave proteins selectively at specific peptide bonds formed by the hydrophobic residues tryptophan, phenylalanine and tyrosine.

Trypsin Chymotrypsin Mix is a basic protein with a molecular wt of around 24000 Daltons. Proteolytic enzymes have been widely used as anti -inflammatory agents.

Trypsin Chymotrypsin Mix is used a NSAID (Non Steroidal Anti Inflammatory Drug). Reduction of inflammation and edema may be described due to the dissolution of soft fibrin and to the clearance of proteinecious debris found in inflammatory exudates.

Trypsin Chymotrypsin Mix when consumed in unprotected form is destroyed by acid in the stomach. However, enteric -coating of tablet, enable the enzyme to pass through the stomach unchanged, and be absorbed in the intestine.

Trypsin Chymotrypsin Mix is also used in ointment form for various treatments.

Pharmaceutical Properties and Therapeutic Applications: