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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-6-29
pubmed:abstractText
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 [(3)H]gibberellin A(1) (GA(1)) to a soluble macromolecular component present in the cytosol was demonstrated at 4 degrees 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 (3)H-activity bound to this protein was largely [(3)H]GA(1) and not a metabolite. Binding was pH sensitive but only a small percentage (20%) appeared to be exchangeable on addition of unlabeled GA(1). Both biologically active and inactive GAs and non-GAs were able to inhibit GA(1) binding. [(3)H]GA(1) 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.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Dec
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
934-41
pubmed:dateRevised
2010-9-15
pubmed:year
1987
pubmed:articleTitle
In Vitro Gibberellin A(1) Binding in Zea mays L.
pubmed:affiliation
Plant Growth Laboratory and Department of Vegetable Crops, University of California, Davis, California 95616.
pubmed:publicationType
Journal Article