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The purification of cytokinin oxidase from Zea mays kernels

Cytokinin oxidase has been purified to apparent homogeneity from Zea mays kernels as indicated by a single protein staining spot on a 2-D, IEF/SDS PAGE gel. Polyclonal antibodies raised to this protein were able to precipitate cytokinin oxidase activity from a highly active, partially purified (QAE-...

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Bibliographic Details
Published in:Phytochemistry (Oxford) 1989, Vol.28 (5), p.1313-1319
Main Authors: Burch, Lindsay R., Horgan, Roger
Format: Article
Language:English
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Summary:Cytokinin oxidase has been purified to apparent homogeneity from Zea mays kernels as indicated by a single protein staining spot on a 2-D, IEF/SDS PAGE gel. Polyclonal antibodies raised to this protein were able to precipitate cytokinin oxidase activity from a highly active, partially purified (QAE-Sephadex) preparation in the presence of fixed Staphylococcus aureus cells. The polyclonal antibodies raised to cytokinin oxidase from Z. mays crossreact with a similar protein in partially purified cytokinin oxidase preparations from dried wheat seeds.
ISSN:0031-9422
1873-3700
DOI:10.1016/S0031-9422(00)97737-9