A new serine proteinase inhibitor, mustard trypsin inhibitor 2 (MTI-2), has been isolated from white mustard (Sinapis alba L.) seed by affinity chromatography and reverse phase HPLC. The protein inhibits the catalytic activity of bovine β-trypsin and bovine α-chymotrypsin, with dissociation constants (Kd) of 1.6 × 10-10 M and 5.0 × 10-7 M, respectively, at pH 8.0 and 21°C, the stiochiometry of both proteinase-inhibitor complexes being 1:1. The amino acid sequence of MTI-2, which was determined following S-pyridylethylation, is comprised of 63 residues, corresponding to a molecular weight of about 7 kDa, and shows only extremely limited homology to other serine proteinase inhibitors.
Purification, inhibitory properties and amino acid sequence of a new serine proteinase inhibitor from white musterd (Sinapis alba L.) seed / E. Menegatti, G. Tedeschi, S. Ronchi, F. Bortolotti, P. Ascenzi, R.M. Thomas, M. Bolognesi, S. Palmieri.. - In: FEBS LETTERS. - ISSN 0014-5793. - 301:1(1992), pp. 10-14.
Purification, inhibitory properties and amino acid sequence of a new serine proteinase inhibitor from white musterd (Sinapis alba L.) seed
G. Tedeschi;S. Ronchi;M. Bolognesi;
1992
Abstract
A new serine proteinase inhibitor, mustard trypsin inhibitor 2 (MTI-2), has been isolated from white mustard (Sinapis alba L.) seed by affinity chromatography and reverse phase HPLC. The protein inhibits the catalytic activity of bovine β-trypsin and bovine α-chymotrypsin, with dissociation constants (Kd) of 1.6 × 10-10 M and 5.0 × 10-7 M, respectively, at pH 8.0 and 21°C, the stiochiometry of both proteinase-inhibitor complexes being 1:1. The amino acid sequence of MTI-2, which was determined following S-pyridylethylation, is comprised of 63 residues, corresponding to a molecular weight of about 7 kDa, and shows only extremely limited homology to other serine proteinase inhibitors.
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