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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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Published in: | Phytochemistry (Oxford) 1989, Vol.28 (5), p.1313-1319 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 0031-9422 1873-3700 |
DOI: | 10.1016/S0031-9422(00)97737-9 |