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 β-trypsin and bovine α-chymotrypsin with apparent dissociation constants of 3.0 × 10-10 M and 4.1 × 10-7 M, at pH 8.0 and 21°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 Mr, of about 6.7 kDa. The p1-pi, 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.
| Original language | English |
|---|---|
| Pages (from-to) | 221-224 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 342 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Apr 4 1994 |
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Keywords
- Amino acid sequence
- Brassica napus var. oleifera
- Rapeseed
- Serine proteinase inhibitor
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Purification, inhibitory properties, amino acid sequence and identification of the reactive site of a new serine proteinase inhibitor from oil-rape (itBrassica napus) seed. / Ceciliani, Fabrizio; Bortolotti, Fabrizio; Menegatti, Enea; Ronchi, Severino; Ascenzi, Paolo; Palmieri, Sandro.
In: FEBS Letters, Vol. 342, No. 2, 04.04.1994, p. 221-224.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification, inhibitory properties, amino acid sequence and identification of the reactive site of a new serine proteinase inhibitor from oil-rape (itBrassica napus) seed
AU - Ceciliani, Fabrizio
AU - Bortolotti, Fabrizio
AU - Menegatti, Enea
AU - Ronchi, Severino
AU - Ascenzi, Paolo
AU - Palmieri, Sandro
PY - 1994/4/4
Y1 - 1994/4/4
N2 - 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 β-trypsin and bovine α-chymotrypsin with apparent dissociation constants of 3.0 × 10-10 M and 4.1 × 10-7 M, at pH 8.0 and 21°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 Mr, of about 6.7 kDa. The p1-pi, 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.
AB - 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 β-trypsin and bovine α-chymotrypsin with apparent dissociation constants of 3.0 × 10-10 M and 4.1 × 10-7 M, at pH 8.0 and 21°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 Mr, of about 6.7 kDa. The p1-pi, 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.
KW - Amino acid sequence
KW - Brassica napus var. oleifera
KW - Rapeseed
KW - Serine proteinase inhibitor
UR - http://www.scopus.com/inward/record.url?scp=0028219989&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028219989&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(94)80505-9
DO - 10.1016/0014-5793(94)80505-9
M3 - Article
C2 - 8143882
AN - SCOPUS:0028219989
VL - 342
SP - 221
EP - 224
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2
ER -