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A trypsin inhibitor from snail medic seeds active against pest proteases.
- Source :
-
Phytochemistry [Phytochemistry] 1997 Feb; Vol. 44 (3), pp. 393-8. - Publication Year :
- 1997
-
Abstract
- A protein trypsin inhibitor from seeds of snail medic (Medicago scutellata), MsTI, has been purified by ion-exchange chromatography, gel-filtration chromatography and reverse-phase HPLC. The protein inhibits the catalytic activity of bovine beta-trypsin, with an apparent Kd of 1.8 x 10(-9), but exhibits no activity towards bovine alpha-chymotrypsin. Moreover, MsTI inhibits the trypsin-like proteinase activity present in larvae of the crop pests Adoxophyes orana, Hyphantria cunea, Lobesia botrana and Ostrinia nubilalis. The complete amino acid sequence of MsTI consists of 62 residues corresponding to a M(r) of 6925. Sequence comparison shows that MsTI exhibits significant similarity to other proteins belonging to the Bowman-Birk trypsin inhibitor family, and the closest identity (81%) with the wound-induced trypsin inhibitor from Medicago sativa leaves.
- Subjects :
- Amino Acid Sequence
Animals
Catalysis
Cattle
Chromatography, Gel
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Electrophoresis, Capillary
Molecular Sequence Data
Protease Inhibitors isolation & purification
Sequence Homology, Amino Acid
Trypsin metabolism
Trypsin Inhibitors isolation & purification
Lepidoptera enzymology
Medicago sativa chemistry
Protease Inhibitors pharmacology
Trypsin Inhibitors pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 0031-9422
- Volume :
- 44
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Phytochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 9014368
- Full Text :
- https://doi.org/10.1016/s0031-9422(96)00483-9