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Purification, inhibitory properties, amino acid sequence and identification of the reactive site of a new serine proteinase inhibitor from oil-rape (itBrassica napus) seed
- Source :
- FEBS Letters. 342:221-224
- Publication Year :
- 1994
- Publisher :
- Wiley, 1994.
-
Abstract
- A new serine proteinase inhibitor, rapeseed trypsin inhibitor (RTI), has been isolated from rapeseed (Brassica napus var. oleifera) seed. The protein inhibits the catalytic activity of bovine beta-trypsin and bovine alpha-chymotrypsin with apparent dissociation constants of 3.0 x 10(-10) M and 4.1 x 10(-7) M, at pH 8.0 and 21 degrees C, respectively. The stoichiometry of both proteinase-inhibitor complexes is 1:1. The amino acid sequence of RTI consists of 60 amino acid residues, corresponding to an M(r) of about 6.7 kDa. The P1-P1' reactive site bond has been tentatively identified at position Arg20-Ile21. RTI shows no similarity to other serine proteinase inhibitors except the low molecular weight mustard trypsin inhibitor (MTI-2). RTI and MTI-2 could be members of a new class of plant serine proteinase inhibitors.
- Subjects :
- Stereochemistry
Trypsin inhibitor
Molecular Sequence Data
Biophysics
Brassica
Biochemistry
Rapeseed
Serine
Structural Biology
Genetics
Amino Acid Sequence
Molecular Biology
Peptide sequence
Plant Proteins
chemistry.chemical_classification
Binding Sites
Plants, Medicinal
Sequence Homology, Amino Acid
biology
Serine proteinase inhibitor
Cell Biology
biology.organism_classification
Brassica napus var. oleifera
Dissociation constant
Enzyme
chemistry
Enzyme inhibitor
Seeds
biology.protein
Serine Proteinase Inhibitors
Trypsin Inhibitors
human activities
Mustard Plant
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 342
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....cb5d15b60bbd0d738c4efce1891232f3
- Full Text :
- https://doi.org/10.1016/0014-5793(94)80505-9