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231224s1985 xx |||||o 00| ||eng c |
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|a 10.1016/S0176-1617(85)80196-6
|2 doi
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|a pubmed24n0743.xml
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|a (NLM)23196079
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|a (PII)S0176-1617(85)80196-6
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a van Staden, J
|e verfasserin
|4 aut
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|a Peroxidase and zeatin stability
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|c 1985
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 03.12.2012
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|a Date Revised 30.09.2020
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|a published: Print-Electronic
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|a Citation Status PubMed-not-MEDLINE
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|a Copyright © 1985 Gustav Fischer Verlag, Stuttgart. Published by Elsevier GmbH.. All rights reserved.
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|a Authentic (14)C-zeatin was subjected to various enzymatic and chemical treatments (in vitro). The treatments included addition of peroxidase and hydrogen peroxide separately and in combination and resulted in all cases, in breakdown of the authentic zeatin. This breakdown was in-creased where hydrogen peroxide was added to the reaction mixture. Oxidation of zeatin thus resulted in the detection of three new peaks of radioactivity, the most polar of which did not co-elute with any of the authentic markers tested and was not biologically active. The two less polar peaks detected co-eluted with authentic adenine and 6-(2,3,4-trihydroxy-3-methylbutyl-amino)-purine. Of these the latter compound stimulated the division of soybean callus
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|a Journal Article
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|a Forsyth, C
|e verfasserin
|4 aut
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|i Enthalten in
|t Journal of plant physiology
|d 1979
|g 118(1985), 4 vom: 01. März, Seite 367-71
|w (DE-627)NLM098174622
|x 1618-1328
|7 nnns
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| 773 |
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|g volume:118
|g year:1985
|g number:4
|g day:01
|g month:03
|g pages:367-71
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|u http://dx.doi.org/10.1016/S0176-1617(85)80196-6
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|d 118
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