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Elicitor-induced Tyrosine Decarboxylase from Plant Cell Suspension Cultures. Part I. Induction and Purification
Institute of Biotechnology, ETH-H6nggerberg, CH-8093 Ztirich, Switzerland.ORCID iD: 0000-0001-8899-5046
1988 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 88, p. 46-51Article in journal (Refereed) Published
Abstract [en]

L-Tyrosine decarboxylase (EC 4.1.1.25) activity was induced in cellsuspension cultures of Thalictrum rugosum Ait. and Eschscholtzia californicaCham. with a yeast polysaccharide preparation (elicitor). Thehighest L-tyrosine decarboxylase activity in extracts from 7-day-old cellcultures of E. californica was observed 5 hours after addition of 30 to 40micrograms elicitor per gram cell fresh weight. The enzyme extractedfrom cells of E. californica was purified 1540-fold to a specific activityof 2.6 micromoles CO2 produced per minute per millim protein at pH8A and 30°C. Purified enzyme from T. rugosum showed a specific activityof 0.18 micromoles per minute per milligram protein. The purificationprocedure involved ammonium sulfate fractionation, anion-exchange fastprotein liquid chromatography, ultrafiltration, and hydrophobic interactionchromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresisshowed that the enzyme from the two plant cell cultures hadsubunits of identical molecular weight (56,300 1 300 daltons. 

Place, publisher, year, edition, pages
1988. Vol. 88, p. 46-51
National Category
Biochemistry and Molecular Biology
Research subject
Natural Science, Biochemistry
Identifiers
URN: urn:nbn:se:lnu:diva-602OAI: oai:DiVA.org:lnu-602DiVA, id: diva2:307332
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2017-12-12Bibliographically approved

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Brodelius, Peter

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