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Biosynthesis and degradation of a wheat embryo cytokinin-binding protein during embryogenesis and germination
The accumulation and degradation of a wheat (Triticum durum) embryo cytokinin-binding protein (CBF-1) was followed during embryo development and germination by its $\text{N}^{6}$-benzyladenine (BA) binding activity and immunological reactivity (rocket immunoelectrophoresis and Western blotting). Bot...
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Published in: | Plant physiology (Bethesda) 1985-11, Vol.79 (3), p.706-710 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that cite this one |
Online Access: | Get full text |
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Summary: | The accumulation and degradation of a wheat (Triticum durum) embryo cytokinin-binding protein (CBF-1) was followed during embryo development and germination by its $\text{N}^{6}$-benzyladenine (BA) binding activity and immunological reactivity (rocket immunoelectrophoresis and Western blotting). Both BA binding activity and CBF-1 appeared at 2 weeks post-anthesis and rose sharply between 2 to 4 weeks before leveling off to approximately 47 micrograms per embryo (9% of the soluble embryo protein at maturity). In vitro translation of polyadenylated RNA from 20-day-old embryos yielded a polypeptide which was immunoprecipitable with anti-CBF-1 IgG and migrated closely to the 54-kilodalton CBF-1 polypeptide on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Upon germination, both the amount of CBF-1 and BA binding activity dropped to low levels within 3 days. The data are discussed in relation to the possible role of CBF-1 as a regulator of cytokinin availability, and comparisons are drawn between the structural and biosynthetic similarities found between CBF-1 and the vicilin storage proteins of legumes. An improved method for isolating undegraded CBF-1 from whole seeds is also presented. |
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ISSN: | 0032-0889 1532-2548 |
DOI: | 10.1104/pp.79.3.706 |