Identification and localization of an active cutinase in the pollen of Brassica napus L. View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-04

AUTHORS

Simon J. Hiscock, Frances M. Dewey, Julian O. D. Coleman, Hugh G. Dickinson

ABSTRACT

Polyclonal antiserum and monoclonal antibodies raised to a purified cutinase from Fusarium solani f. sp. pisi have been used to identify an active cutinase in the pollen of Brassica napus. These antibodies recognized a polypeptide with an estimated molecular weight of 22kDa — a molecular weight indentical to that of the Fusarium cutinase — and localized this polypeptide to the intine of the pollen wall. Enzyme assays on the renatured 22kDa polypeptide after electroelution from a preparative SDS-PAGE gel revealed the polypeptide to be an enzyme capable of catalysing the hydrolysis of tritiated apple cutin and the synthetic substrate p-nitrophenyl butyrate. The molecular weight, immunological properties and substrate specificity of the Brassica cutinase suggest that this enzyme resembles more closely fungal cutinases than it does the cutinase from the pollen of Nasturtium (Tropaeolum majus) — the only angiosperm cutinase so far characterized (Maiti et al., 1979, Arch. Biochem. Biophys. 196, 412–423). These differences between the pollen cutinases from two members of the Dicotyledoneae are unexpected and predict a diversity of this class of pollen enzyme within the angiosperms. More... »

PAGES

377-384

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00201816

DOI

http://dx.doi.org/10.1007/bf00201816

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1006555381


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