De novo sequencing and characterization of a novel Bowman-Birk inhibitor from Lathyrus sativus L. seeds by electrospray mass spectrometry(385 views) Tamburino R, Severino V, Sandomenico A, Ruvo M, Parente A, Chambery A, Di Maro A
Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, Second University of Naples, I-81100 Caserta, Italy
Institute of Biostructures and Bioimaging-IBB, CNR, I-80134, Napoli, Italy
Institute of Crystallography, CNR, I-70126, Bari, Italy
References: Birk, Y., (2003) Plant Protease Inhibitors: Significance in Nutrition, Plant Protection, Cancer Prevention and Genetic Engineering, , Springer-Verlag, Berlin Heidelberg New Yor
Laskowski Jr., M., Kato, I., (1980) Annu. Rev. Biochem., 49, pp. 593-626
Birk, Y., (1985) Int. J. Pept. Protein Res., 25, pp. 113-131
Clemente, A., Domoney, C., (2006) Curr. Protein Pept. Sci., 7, pp. 201-216
Odani, S., Ikenaka, T., (1973) J. Biochem., 74, pp. 697-715
Qi, R.F., Song, Z.W., Chi, C.W., (2005) Acta Biochim. Biophys. Sin. (Shanghai), 37, pp. 283-292
Rocco, M., Livia Malorni, L., Chambery, A., Poerio, E., Parente, A., Di Maro, A., (2011) Mol. BioSyst., 7, pp. 2500-2507
De Azevedo Pereira, R., Valencia-Jimenez, A., Magalhaes, C.P., Prates, M.V., Melo, J.A., De Lima, L.M., De Sales, M.P., Grossi-De-Sa, M.F., (2007) J. Agric. Food Chem., 55, pp. 10714-10719
Di Maro, A., Chambery, A., Carafa, V., Costantini, S., Colonna, G., Parente, A., (2009) Biochimie, 91, pp. 352-363
Castellano, I., Ruocco, M.R., Cecere, F., Di Maro, A., Chambery, A., Michniewicz, A., Parlato, G., De Vendittis, E., (2008) Biochim. Biophys. Acta, 1784, pp. 816-826
Poerio, E., Di Gennaro, S., Di Maro, A., Farisei, F., Ferranti, P., Parente, A., (2003) Biol. Chem., 384, pp. 295-304
Yakoby, N., Raskin, I., (2004) J. Biochem. Biophys. Methods, 59, pp. 241-251
Marinec, P.S., Chen, L., Barr, K.J., Mutz, Mitchell.W., Gerald, R.C., Gestwicki, J.E., (2009) Proc. Nat. Acad Sci., 106, pp. 1336-1341
Chambery, A., Di Maro, A., Parente, A., (2008) Phytochemistry, 69, pp. 1973-1982
Prasad, E.R., Dutta-Gupta, A., Padmasree, K., (2010) Phytochemistry, 71, pp. 363-372
Chambery, A., De Donato, A., Bolognesi, A., Polito, L., Stirpe, F., Parente, A., (2006) Biol. Chem., 387, pp. 1261-1266
Severino, V., Chambery, A., Vitiello, M., Cantisani, M., Galdiero, S., Galdiero, M., Malorni, L., Parente, A., J. Proteome Res., 9, pp. 1050-1062
Li De La Sierra, I., Quillien, L., Flecker, P., Gueguen, J., Brunie, S., (1999) J. Mol. Biol., 285, pp. 1195-1207
Melo, F., Feytmans, E., (1998) J. Mol. Biol., 277, pp. 1141-1152
Syka, J.E., Coon, J.J., Schroeder, M.J., Shabanowitz, J., Hunt, D.F., (2004) Proc. Natl. Acad. Sci. U. S. A., 101, pp. 9528-9533
Ramasarma, P.R., Appu Rao, A.G., Rao, D.R., (1994) J. Agric. Food Chem., 42, pp. 2139-2146
Chambery, A., Pisante, M., Di Maro, A., Di Zazzo, E., Ruvo, M., Costantini, S., Colonna, G., Parente, A., (2007) Proteins, 67, pp. 209-218
De novo sequencing and characterization of a novel Bowman-Birk inhibitor from Lathyrus sativus L. seeds by electrospray mass spectrometry
Bowman-Birk serine protease inhibitors (BBIs) from legume seeds are small proteins showing a two-head structure with distinct reactive site loops, which inhibit two molecules of the same enzyme or two different proteases. Purification and characterization of new BBIs is of broad interest for understanding the basic molecular mechanisms underlying natural defence against the action of proteolytic enzymes. In this study, two novel acidic BBIs (LSI-1a and LSI-2a) were isolated from L. sativus seeds using classical biochemical techniques and characterized for their inhibitory activity. In addition, the N-terminal sequencing of LSI-1a was performed by Edman degradation up to residue 10 and the complete primary structure of the most abundant form (LSI-2a) was determined by using a combination of mass spectrometry approaches, including MALDI-TOF MS, tandem MS and Electron Transfer Dissociation coupled with Proton Transfer Reaction (ETD/PTR) top-down sequencing of N- and C-termini. Furthermore, the LSI-2a dimerization surface has also been investigated by a combination of gel filtration, electrophoretic techniques and homology modelling. Knowing the structure of small proteins inhibiting proteolytic enzymes is of general importance for understanding the defence mechanisms against degradation for their use in biological applications as well as for designing artificial inhibitors.
De novo sequencing and characterization of a novel Bowman-Birk inhibitor from Lathyrus sativus L. seeds by electrospray mass spectrometry
No results.
De novo sequencing and characterization of a novel Bowman-Birk inhibitor from Lathyrus sativus L. seeds by electrospray mass spectrometry
Kállay C, Dávid A, Timári S, Nagy EM, Sanna D, Garribba E, Micera G, De Bona P, Pappalardo G, Rizzarelli E, Sóvágó I * Copper(II) complexes of rat amylin fragments(357 views) Dalton T (ISSN: 1477-9234, 1477-9226, 1477-9234electronic), 2011 Oct 14; 40(38): 9711-9721. Impact Factor:3.838 ViewExport to BibTeXExport to EndNote
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(449 views) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 ViewExport to BibTeXExport to EndNote