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Trypsin inhibitor



Trypsin inhibitors are chemicals that reduce the bio-availability of trypsin, an enzyme essential to nutrition of many animals, including humans.

There are four commercial sources of trypsin inhibitors.

Source Molecular weight Inhibitatory power Details
Serum (α1-antitrypsin) 52 kDa Also known as serum trypsin inhibitor
Lima beans 8-10 kDa 2.2 times weight There are six different lima bean inhibitors.
Bovine pancreas 6.5 kDa 2.5 times weight Kunitz inhibitor is the best known pancreatic inhibitor. Chymotrypsin is also inhibited by this chemical, but less tightly. When extracted from lung tissue, this is known as aprotinin.
Ovomucoid 8-10 kDa 1.2 times weight Ovomucoids are the glycoprotein protease inhibitors found in avian egg white. There are other protease inhibitors in ovomucoids as well.
Soybeans 20.7-22.3 kDa 1.2 times weight Soybeans contain several inhibitors; the one in the chart is considered the primary one. All of them bind chymotryptin to a lesser degree.

See also

References

  • Jones et al., Biochem., 2, 66, (1963)
  • Lineweaver and Murray JBC, 171, 565 (1947)
  • Kunitz and Northrop J. Gen. Physiol., 19, 991 (1936)
  • Fraenkel-Conrat, et al., Arch. Biochem. Biophys., 37, 393 (1952)
  • Frattali, V., and Steiner, R.: Biochem., 7, 521 (1968)
v • d • e
Pharmacology: enzyme inhibition
ClassCompetitive inhibition - Uncompetitive inhibition - Non-competitive inhibition - Suicide inhibition - Mixed inhibition
SubstrateAcetylcholinesterase inhibitors - Aromatase inhibitors - Carbonic anhydrase inhibitors - Integrase inhibitor - Kinase inhibitors - Lipoxygenase inhibitor - Monoamine oxidase inhibitors - Reverse transcriptase inhibitors - Phosphodiesterase inhibitors - Protease inhibitors (ACE inhibitor, Trypsin inhibitor)
 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Trypsin_inhibitor". A list of authors is available in Wikipedia.
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