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Titolo:
Biochemical characterization and N-terminal sequences of two new trypsin inhibitors from Copaifera langsdorffii seeds
Autore:
Silva, JA; Macedo, MLR; Novello, JC; Marangoni, S;
Indirizzi:
Univ Estadual Campinas, UNICAMP, Dept Bioquim, Inst Biol, BR-13083970 Campinas, SP, Brazil Univ Estadual Campinas Campinas SP Brazil BR-13083970 BCpinas, SP, Brazil Univ Fed Mato Grosso do Sul, Dept Ciencias Nat CEUL, Tres Lagoas, MS, Brazil Univ Fed Mato Grosso do Sul Tres Lagoas MS Brazil res Lagoas, MS, Brazil
Titolo Testata:
JOURNAL OF PROTEIN CHEMISTRY
fascicolo: 1, volume: 20, anno: 2001,
pagine: 1 - 7
SICI:
0277-8033(200101)20:1<1:BCANSO>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID SEQUENCES; PROTEINASE-INHIBITOR; PROTEASE INHIBITORS; BLOOD-COAGULATION; PURIFICATION;
Keywords:
Copaifera langsdorffii; seeds; Caesalpinoideae; trypsin inhibitor; N-terminal sequence;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Marangoni, S Univ Estadual Campinas, UNICAMP, Dept Bioquim, Inst Biol, BR-13083970 Campinas, SP, Brazil Univ Estadual Campinas Campinas SP Brazil BR-13083970 BCazil
Citazione:
J.A. Silva et al., "Biochemical characterization and N-terminal sequences of two new trypsin inhibitors from Copaifera langsdorffii seeds", J PROTEIN C, 20(1), 2001, pp. 1-7

Abstract

Two new trypsin inhibitors, TDI-I and TDI-II, were purified from the seedsof the native Brazilian tree Copaifera langsdourfii (Caesalpinoideae, Leguminosae). The purification procedure involved ammonium sulfate fractionation, ion-exchange chromatography on DEAE-Sepharose, affinity chromatography on trypsin-Sepharose, and reversed-phase (RP) HPLC. RP-HPLC yielded two forms (TDI-I and TDI-II), as confirmed by isoelectric focusing, with pi values between 7.0 and 8.1. The molecular mass of the TDI forms was 24 kDa based on FPLC gel filtration on Superdex 75. Under reducing conditions in tricine SDS-PAGE the molecular masses of TDI-I and TDI-II were 12 and 10 kDa, respectively. The k(i) values were 1.1 and 1.2 nM for TDI-I and TDI-II, respectively, and there was no inhibitory effect on chymotrypsin. Amino acid analysis revealed high levels of aspartic acid, glutamic acid, serine, glycine, proline, and lysine but low levels of methionine and aromatic amino acids inboth inhibitors; the calculated molecular masses were 11,456 and 10,008 for TDI-I and II, respectively. Eased on the N-terminal sequences of TDI-I and TDI-II, TDI-I belongs to the Kunitz family of trypsin inhibitors, whereasTDI-II showed no homology to any other protein. This observation suggests that TDI-II belongs to a new inhibitor subclass of low-molecular mass proteins in the subfamily Caesalpinoideae.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 14:22:54