Trypsin inhibitor
From Wikipedia, the free encyclopedia
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 |
| Serum (α1-antitrypsin) | 52 kDa | |
| Lima Beans | 8-10 kDa | 2.2 times weight |
| Bovine Pancreas | 6.5 kDa | 2.5 times weight |
| Ovomucoid | 8-10 kDa | 1.2 times weight |
| Soybeans | 20.7-22.3 kDa | 1.2 times weight |
There are six different lima bean inhibitors.
Ovomucoids are the glycoprotein protease inhibitors found in avian egg white. There are other protease inhibitors in ovomucoids as well.
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.
Soybeans contain several inhibitors; the one in the chart is considered the primary one. All of them bind chymotryptin to a lesser degree.
[edit] See also
- α1-Antitrypsin (serum trypsin inhibitor)
- Serine protease inhibitor
- Protease inhibitor
[edit] 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)
