Characterization of low-molecular-mass trypsin isoinhibitors from oil-rape (Brassica napus var. oleifera) seed (Articolo in rivista)

Type
Label
  • Characterization of low-molecular-mass trypsin isoinhibitors from oil-rape (Brassica napus var. oleifera) seed (Articolo in rivista) (literal)
Anno
  • 1999-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1046/j.1432-1327.1999.00275.x (literal)
Alternative label
  • Ascenzi, P; Ruoppolo, M; Amoresano, A; Pucci, P; Consonni, R; Zetta, L; Pascarella, S; Bortolotti, F; Menegatti, E (1999)
    Characterization of low-molecular-mass trypsin isoinhibitors from oil-rape (Brassica napus var. oleifera) seed
    in European journal of biochemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ascenzi, P; Ruoppolo, M; Amoresano, A; Pucci, P; Consonni, R; Zetta, L; Pascarella, S; Bortolotti, F; Menegatti, E (literal)
Pagina inizio
  • 275 (literal)
Pagina fine
  • 284 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.1999.00275.x/pdf (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 261 (literal)
Rivista
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Consonni, R, Zetta, L. ISMAC Milano (literal)
Titolo
  • Characterization of low-molecular-mass trypsin isoinhibitors from oil-rape (Brassica napus var. oleifera) seed (literal)
Abstract
  • A new low-molecular-mass (6767.8 Da) serine proteinase isoinhibitor has been isolated from oil-rape (Brassica napus var. oleifera) seed, designated 5-oxoPro1-Gly62-RTI-III. The 5-oxoPro1-Gly62-RTI-III isoinhibitor is longer than the Asp2-Pro61-RTI-III and the Ser3-Pro61-RTI-III forms, all the other amino acid residues being identical. In RTI-III isoinhibitors, the P-1-P-1' reactive site bond (where residues forming the reactive site have been identified as P-n...P-1 and P-1'...P-n', where P-1-P-1' is the inhibitor scissile bond) has been identified at position Arg21-Ile22. The inhibitor disulphide bridges pattern has been determined as Cys5-Cys27, Cys18-Cys31, Cys42-Cys52 and Cys54-Cys57. The disulphide bridge arrangement observed in the RTT-III isoinhibitors is reminiscent of that found in a number of toxins (e.g. erabutoxin b). Moreover, the organization of the three disulphide bridges subset Cys5-Cys27, Cys18-Cys31 and Cys42-Cys52 is reminiscent of that found in epidermal growth factor domains. Preliminary H-1-NMR data indicates the presence of alpha alpha NOEs and 3J alpha NH coupling constants, typical of the beta-structure(s). These data suggest that the three-dimensional structure of the RTI-III isoinhibitors may be reminiscent of that of toxins and epidermal growth factor domains, consisting of three-finger shaped loops extending from the crossover region. Values of the apparent association equilibrium constant for RTI-III isoinhibitors binding to bovine P-trypsin and bovine a-chymotrypsin are 3.3 x 10(9) M-1 and 2.4 x 10(6) M-1, respectively, at pH 8.0 and 21.0 degrees C. The serine proteinase: inhibitor complex formation is a pH-dependent entropy-driven process. RTI-III isoinhibitors do not show any similarity to other serine proteinase inhibitors except the low molecular mass white mustard trypsin isoinhibitor, isolated from Sinapis alba L. seed (MTI-2). Therefore, RTI-III and MTI-2 isoinhibitors could be members of a new class of plant serine proteinase inhibitors. (literal)
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