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Properties Of Carrot Polyphenoloxidase
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Physiology and Developmental Biology, Comparative Physiology.
1995 (English)In: Phytochemistry, ISSN 0031-9422, E-ISSN 1873-3700, Vol. 39, no 1, 33-38 p.Article in journal (Refereed) Published
Abstract [en]

A latent phenoloxidase (PPO) was purified in the presence of protease inhibitors from carrot cells to electrophoretic homogeneity. The inactive enzyme had a M(r) of ca 59 000 under denaturating conditions as judged by SDS-PAGE. When stored in the absence of protease inhibitors, PPO in a crude extract was converted to forms with a lower M(r). Phenol oxidase activity of the purified PPO was induced by the presence in the assay medium of 12.5 mM Tris, and 6 mM CaCl2 increased the activity further.

Place, publisher, year, edition, pages
1995. Vol. 39, no 1, 33-38 p.
Keyword [en]
Daucus Carota, Umbelliferae, Carrot, Latent Enzyme, Phenoloxidase, Prophenoloxidase, Purification, Broad Bean Polyphenoloxidase, Glandular Trichomes, Cell-Cultures, Oxidase, Purification, Expression, Activation, Cleavage, Prophenoloxidase, Proteins
National Category
Botany
Identifiers
URN: urn:nbn:se:uu:diva-82824DOI: 10.1016/0031-9422(94)00918-JISI: A1995RB04800006OAI: oai:DiVA.org:uu-82824DiVA: diva2:110731
Available from: 2006-10-13 Created: 2006-10-13 Last updated: 2014-08-13Bibliographically approved

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Söderhäll, Irene

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