Trypsin and Chymotrypsin

[Yomna88]

A mother of a newborn is prescribed w combination medication of trypsin 5mg and chymotrypsin 5mg three times daily before food. Is it safe on breastfeeding? I was unable to find any information regarding its use.

[bestellen]

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.