Characterization and Localization of a Phenoloxidase in Mung Bean Hypocotyl Cell Walls.

Abstract:

:The occurrence of proteins able to oxidize polyphenols even in the absence of H2O2 was recently reported in mung bean (Vigna radiata L.) hypocotyl cell wall extracts (R. Goldberg, A. Chabanet, A.M. Catesson [1993] In K.G. Welinder, S.K. Rasmussen, C. Penel, H. Greppin, eds, Plant Peroxidases: Biochemistry and Physiology, pp. 296-300). Therefore, the possible presence of a laccase in the extracts was investigated using immunocytological and biochemical approaches. An enzyme catalyzing phenol oxidation in the presence of molecular O2 was extracted and purified from the cell walls. This 38-kD cationic protein, like o-diphenoloxidases, was unable to oxidize p-diphenols or p-diamines. However, it crossreacted with an anti-laccase antiserum and, like laccases, its activity was inhibited by N-cetyl-N,N,N-trimethylammonium bromide but not by ferulic acid salts. Immunolabeling data showed that the 38-kD oxidase was absent from all cellulosic cell walls. It was localized only in lignifying and lignified cell walls. This restricted localization suggests that this laccase-like phenoloxidase could participate in the lignification process but not in the primary wall stiffening, which develops in the epidermal and cortical tissues along the mung bean hypocotyl.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Chabanet A,Goldberg R,Catesson AM,Quinet-Szely M,Delaunay AM,Faye L

doi

10.1104/pp.106.3.1095

subject

Has Abstract

pub_date

1994-11-01 00:00:00

pages

1095-1102

issue

3

eissn

0032-0889

issn

1532-2548

pii

106/3/1095

journal_volume

106

pub_type

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