Identification and characterization of a Bowman-Birk inhibitor active towards trypsin but not chymotrypsin in Lupinus albus seeds

Phytochemistry

Volumn 69, Issue 9, 2008, Pages 1820-1825

  Scarafoni, Alessio ^a   Consonni, Alessandro ^a   Galbusera, Valerio ^a   Negri, Armando ^a   Tedeschi, Gabriella ^a   Rasmussen, Patrizia ^a   Magni, Chiara ^a   Duranti, Marcello ^a  

^a UNIVERSITY OF MILAN   (Italy)

Author keywords

Antitryptic activity; Bowman Birk inhibitor; Legume seeds; Lupinus albus; Protein purification

Indexed keywords

BOWMAN BIRK INHIBITOR; CHYMOTRYPSIN; TRYPSIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; DRUG ANTAGONISM; ISOLATION AND PURIFICATION; KINETICS; LUPIN; MASS SPECTROMETRY; METABOLISM; MOLECULAR GENETICS; PH; PLANT SEED; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; TEMPERATURE; TITRIMETRY;

AMINO ACID SEQUENCE; CHYMOTRYPSIN; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; KINETICS; LUPINUS; MOLECULAR SEQUENCE DATA; SEEDS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TEMPERATURE; TITRIMETRY; TRYPSIN; TRYPSIN INHIBITOR, BOWMAN-BIRK SOYBEAN;

BOVINAE; FABACEAE; LUPINUS ALBUS;

EID: 44549085952     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2008.03.023     Document Type: Article

References (40)

1. Altschul S.F., Madden T.L., Schäffer A.A., Zhang J., Zhang Z., Miller W., and Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucl. Acid Res. 25 (1997) 3389-3402
2. Balestrazzi A., Confalonieri M., Odoardi M., Ressegotti V., Allegro G., Tava A., and Carbonera D. A trypsin inhibitor cDNA from a novel source, snail medic (Medicago scutellata L.): cloning and functional expression in response to wounding, herbivore, jasmonic acid and salicylic acid. Plant Sci. 167 (2004) 337-346
3. Birk Y. Antinutritional factors in lupins and in other legume seeds: pros and cons. In: Neves-Martin J.M., and Beirao da Costa M.L. (Eds). Advances in Lupin Research (1993), ISA Press, Lisboa, Portugal 424-429
4. Bowman D.E. Further identification of bean trypsin inhibiting factors. Arch. Biochem. Biophys. 16 (1948) 109-113
5. Bradford M.A. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 76 (1976) 248-254
6. Brauer A.B.E., Domingo G.J., Cooke R.M., Mattheus S.J., and Leatherbarrow R.J. A conserved cis peptide bond is necessary for the activity of Bowman-Birk inhibitor protein. Biochemistry 41 (2002) 10608-10615
7. Clemente A., and Domoney C. Biological significance of polymorphism in legume protease inhibitors from the Bowman-Birk family. Curr. Prot. Pep. Sci. 7 (2006) 201-216
8. Domash V.I. A protein trypsin inhibitor from seeds of white lupin (Lupinus albus L.). Dokl. Akad. Nauk BSSR 35 (1991) 1039-1041
9. Domoney C. Inhibitors of legume seeds. In: Shewry P.R., and Casey R. (Eds). Seed Proteins (1999), Kluwer Academic Publishers, Amsterdam 635-655
10. Duranti M., Barbiroli A., Scarafoni A., Tedeschi G., and Morazzoni P. One-step purification of Kunitz soybean inhibitor. Protein Exp. Purif. 30 (2003) 167-170
11. Duranti M., Restani P., Poniatowska M., and Cerletti P. The seed globulins of Lupinus albus. Phytochemistry 20 (1981) 2071-2075
12. Egaña J.I., Uauy R., Cassorla X., Barrera G., and Yañez E. Sweet lupin protein quality in young men. J. Nutr. 122 (1992) 2341-2347
13. Gallardo F., Araya H., Pak N., and Tagle M.A. Toxic factors in chilean legumes II. Trypsin inhibitor activity. Arch. Latinoam. Nutr. 24 (1974) 183-189
14. Gasteiger E., Hoogland C., Gattiker A., Duvaud S., Wilkins M.R., Appel R.D., and Bairoch A. Protein identification and analysis tools on the ExPASy server. In: Walker J.M. (Ed). The Proteomics Protocols Handbook (2005), Humana Press, Totowa, New York 571-607
15. Higgins D., Thompson J., Gibson T., Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acid Res. 22 (1994) 4673-4680
16. Hove E.I. Composition and protein quality of sweet lupin seeds. J. Sci. Food Agric. 25 (1974) 851-859
17. Hove E.I., and King S. Trypsin inhibitor content of lupin seeds and other grain legume. New Zeal. J. Agric. Res. 22 (1979) 41-42
18. Kelly S.M., Jess T.J., and Price N.C. How to study proteins by circular dichroism. Biochim. Biophys. Acta 1751 (2005) 119-139
19. Kennedy A.R. Chemopreventive agents: protease inhibitors. Pharmacol. Ther. 78 (1998) 167-209
20. Koiwa H., Bressan R.A., and Hasegawa P.M. Regulation of protease inhibitors and plant defense. Trends Plant Sci. 2 (1997) 379-384
21. Korth K.L., and Dixon R.A. Evidence for chewing insect-specific molecular events distinct from a general wound response in leaves. Plant Physiol. 115 (1997) 1299-1305
22. Laskowsky M., and Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 49 (1980) 593-626
23. Leatherbarrow, R.J., 1992. GraFit. Erithacus Software Ltd., Staines, UK.
24. Magni C., Scarafoni A., Hernle A., Sessa F., Prinsi B., Espen L., and Duranti M. Combined 2D electrophoretic approaches for the study of white lupin mature seed storage proteome. Phytochemistry 68 (2007) 997-1007
25. Mello M.O., Tanaka A.S., and Silva Filho M.C. Molecular evolution of Bowman-Birk type proteinase inhibitors in flowering plants. Mol. Phyl. Evol. 27 (2003) 103-112
26. Mosolov V.V., and Valueva T.A. Proteinase inhibitors and their function in plants: a review. Appl. Biochem. Microbiol. 41 (2005) 227-246
27. Muel, F., Carrouée, B., Grosjean, F., 1998. Trypsin inhibitor activity of pea cultivars: new data and a proposal strategy for breeding programmes. In: AEP (Eds.), Proceedings of the Third European Conference on Grain Legumes, Valladolid, Spain, pp. 164-165.
28. O'Donnell P.J., Calvert C., Atzorn R., Wasternack C., Leyser H.M.O., and Bowles D.J. Ethylene as a signal mediating the wound response of tomato plants. Science 274 (1996) 1914-1917
29. Odani S., and Ikenaka T. Studies on soybean trypsin inhibitors. 8. Disulphide bridges in soybean Bowman-Birk inhibitors. J. Biochem. 74 (1973) 697-715
30. Odani S., and Ikenaka T. Studies on soybean trypsin inhibitors. 15. Change of the inhibitory activity of Bowman-Birk inhibitor upon replacements of the chymotrypsin reactive site serine residue by other amino acids. J. Biochem. 84 (1978) 1-9
31. Piergiovanni A.R., and Galasso I. Polymorphism of trypsin and chymotrypsin binding loops in Bowman-Birk inhibitors from common bean (Phaseolus vulgaris L.). Plant Sci. 166 (2004) 1525-1531
32. Prakash B., Selvaraj S., Murthy M.R.N., Sreerama Y.N., Rao D.R., and Gowda L.R. Analysis of the amino acid sequences of plant Bowman-Birk inhibitors. J. Mol. Evol. 42 (1996) 560-569
33. Qi R.F., Song Z.W., and Chi C.W. Structural features and molecular evolution of Bowman-Birk protease inhibitors and their potential application. Acta Biochim. Biophys. Sin. 37 (2005) 283-292
34. Ragg E.M., Galbusera V., Scarafoni A., Negri A., Tedeschi G., Consonni A., Sessa F., and Duranti M. Inhibitory properties and solution structure of a potent Bowman-Birk protease inhibitor from lentil (Lens culinaris L.) seeds. FEBS J. 273 (2006) 4024-4039
35. Roda A., Halitschke R., Steppuhn A., and Baldwin I.T. Individual variability in herbivore-specific elicitors from the plant's perspective. Mol. Ecol. 13 (2004) 2421-2433
36. Ryan C.A. Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 28 (1990) 425-449
37. Salmanowicz B.P., and Weder J.K.P. Primary structure of 2S albumin from seeds of Lupinus albus. Z. Lebensm. Unters. Forsch. A 204 (1997) 129-135
38. Scarafoni A., Magni C., and Duranti M. Molecular nutraceutics as a mean to investigate the positive effects of legume seed proteins on human health. Trends Food Sci. Technol. 8 (2007) 454-463
39. Schechter J., and Berger A. On the size of the active sites of proteases. Biochem. Biophys. Res. Commun. 27 (1967) 157-162
40. Wilson K.A. The proteolysis of trypsin inhibitor in legume seeds. Crit. Rev. Biotechnol. 8 (1988) 197-216