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Titolo:
Diferulate and lignin formation is related to biochemical differences of wall-bound peroxidases
Autore:
Gonzalez, LF; Rojas, MC; Perez, FJ;
Indirizzi:
Univ Chile, Fac Ciencias, Dept Quim, Santiago, Chile Univ Chile SantiagoChile ile, Fac Ciencias, Dept Quim, Santiago, Chile Univ Chile, Fac Ciencias, Dept Ciencias Ecol, Santiago, Chile Univ Chile Santiago Chile Ciencias, Dept Ciencias Ecol, Santiago, Chile
Titolo Testata:
PHYTOCHEMISTRY
fascicolo: 5, volume: 50, anno: 1999,
pagine: 711 - 717
SICI:
0031-9422(199903)50:5<711:DALFIR>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
LEAF ELONGATION ZONE; CELL-WALL; HYDROGEN-PEROXIDE; SPATIAL-DISTRIBUTION; CROSS-LINKING; TALL FESCUE; COLEOPTILES; ACID; LIGNIFICATION; EXTENSIBILITY;
Keywords:
Avena sativa; Poaceae; oat; enzymology; peroxidase; diferulic acid; lignin;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Gonzalez, LF Univ Chile, Fac Ciencias, Dept Quim, Casilla 653, Santiago, Chile Univ Chile Casilla 653 Santiago Chile 653, Santiago, Chile
Citazione:
L.F. Gonzalez et al., "Diferulate and lignin formation is related to biochemical differences of wall-bound peroxidases", PHYTOCHEM, 50(5), 1999, pp. 711-717

Abstract

Purified cell walls from oat coleoptiles contain ionically and covalently bound peroxidase activity, which correspond to 0.6% of the total peroxidaseactivity in the coleoptile. Ionically wall-bound peroxidases showed a 2-3-fold higher efficacy than peroxidases in the covalent Fraction, in the use of H2O2 and phenolic substrates that are precursors of diferulate bridges and lignin. The NADH oxidase activity in both fractions was effectively enhanced by p-coumaric acid and the ionic fraction showed a higher efficacy over the covalent one for NADH utilization in the presence of this phenol. Moreover, the isoelectrofocusing pattern revealed marked differences in isoform composition for ionically and covalently bound wall peroxidases. A cationic group of isoperoxidases (pI similar to 9.6) was present only in the ionic fraction while the covalent fraction was enriched with anionic forms (pI similar to 4.0-6.5). In excised coleoptiles incubated for 24 h, the ionically wall-bound peroxidase activity increased by 50% over covalently bound activity for 4 h of incubation. The increase of peroxidase activity preceded the accumulation of diferulic acid and lignin in oat cell walls. Thus, the evidence here reported suggest a possible functional difference of peroxidase wall fractions studied related to diferulate and lignin synthesis in oatcoleoptiles. (C) 1998 Elsevier Science Ltd. All rights reserved.

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Documento generato il 22/09/20 alle ore 12:40:29