Purification, inhibitory properties, amino-acid-sequence and identification of the reactive-site of a new serine proteinase- inhibitor from oil-rape (Brassica napus) seed
Articolo
Data di Pubblicazione:
1994
Citazione:
Purification, inhibitory properties, amino-acid-sequence and identification of the reactive-site of a new serine proteinase- inhibitor from oil-rape (Brassica napus) seed / F. Ceciliani, F. Bortolotti, E. Menegatti, S. Ronchi, P. Ascenzi, S. Palmieri. - In: FEBS LETTERS. - ISSN 0014-5793. - 342:2(1994 Apr 04), pp. 221-224.
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.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Seeds ; Mustard Plant ; Plants, Medicinal ; Trypsin Inhibitors ; Molecular Sequence Data ; Amino Acid Sequence ; Sequence Homology, Amino Acid ; Plant Proteins ; Brassica ; Binding Sites
Elenco autori:
F. Ceciliani, F. Bortolotti, E. Menegatti, S. Ronchi, P. Ascenzi, S. Palmieri
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