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. 1987 Dec;85(4):934–941. doi: 10.1104/pp.85.4.934

In Vitro Gibberellin A1 Binding in Zea mays L. 1

Brian Keith 1,2, Lawrence Rappaport 1
PMCID: PMC1054372  PMID: 16665834

Abstract

The first and second leaf sheaths of Zea mays L. cv Golden Jubilee were extracted and the extract centrifuged at 100,000g to yield a supernatant or cytosol fraction. Binding of [3H]gibberellin A1 (GA1) to a soluble macromolecular component present in the cytosol was demonstrated at 4°C by Sephadex G-200 chromatography. The binding component was of high molecular weight (HMW) and greater than 500 kilodaltons. The HMW component was shown to be a protein and the 3H-activity bound to this protein was largely [3H]GA1 and not a metabolite. Binding was pH sensitive but only a small percentage (20%) appeared to be exchangeable on addition of unlabeled GA1. Both biologically active and inactive GAs and non-GAs were able to inhibit GA1 binding. [3H]GA1 binding to an intermediate molecular weight (IMW) fraction (40-100 kilodaltons) was also detected, provided cytosol was first desalted using Sephadex G-200 chromatography. Gel filtration studies suggest that the HMW binding component is an aggregate derived from the IMW fraction. The HMW binding fraction can be separated into two components using anion exchange chromatography.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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