Hysteresis and Cooperative Behavior of a Latent Plant Polyphenoloxidase
Author(s) -
Edelmira Valero,
Francisco Garcı́a-Carmona
Publication year - 1992
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.98.2.774
Subject(s) - vitis vinifera , enzyme , chemistry , substrate (aquarium) , kinetics , lag , enzyme assay , hysteresis , lag time , biochemistry , biophysics , chromatography , botany , biology , biological system , ecology , computer network , physics , quantum mechanics , computer science
Appearance of a lag period dependent on pH in the expression of the catecholase activity of a polyphenoloxidase extracted in a latent state from Airen grape (Vitis vinifera L.) berries, is revealed, suggesting the hysteretic nature of the enzyme. The lag time was independent of enzyme concentration, indicating that slow pH-induced conformational changes in the protein must occur during assay. Results obtained by varying substrate concentration show that the system presents hyperbolic or cooperative kinetics depending on the pH of the assay.
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