Detection of brassinosteroids in pollen of Lolium perenne L. by immunocytochemistry

Taylor, Philip E., Spuck, Kerstin, Smith, Penelope M., Sasse, Jenneth M., Yokota, Takao, Griffiths, Peter G. and Cameron, Donald W. 1993, Detection of brassinosteroids in pollen of Lolium perenne L. by immunocytochemistry, Planta, vol. 189, no. 1, pp. 91-100.

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Title Detection of brassinosteroids in pollen of Lolium perenne L. by immunocytochemistry
Author(s) Taylor, Philip E.
Spuck, Kerstin
Smith, Penelope M.
Sasse, Jenneth M.
Yokota, Takao
Griffiths, Peter G.
Cameron, Donald W.
Journal name Planta
Volume number 189
Issue number 1
Start page 91
End page 100
Total pages 10
Publisher Springer
Place of publication Heidelberg, Germany
Publication date 1993-01
ISSN 0032-0935
1432-2048
Keyword(s) amyloplast (brassinosteroid storage)
brassinosteroid (immunolocalization)
lolium (pollen)
pollen (development, brassinosteroid)
Summary Bioactive brassinosteroids have been localized in developing and mature pollen of anhydrously fixed rye-grass (Lolium perenne) by immunocytochemistry using polyclonal antibodies to castasterone generated in rabbits. Tricellular pollen fixed by freeze-substitution was also labelled in the starch granules. Study of the developmental sequence of the pollen through the microsporocyte, microspore, bicellular and tricellular stages showed that the brassinosteroids were increasingly sequestered in starch granules as the amyloplasts matured, supporting the view that these are storage organelles for these potent plant growth promoters. In bicellular pollen, heavy labelling was seen in the zone within 0.5 μm of the starch granule, where stromal tissue remains. Thus, the stroma may be the site of synthesis of these compounds. During aqueous fixation, the brassinosteroids leached from the starch granules of tricellular pollen, indicating that they would be quickly available after imbibition to influence the physiology of germinating pollen. The results from high-performance liquid chromatography of dansylaminophenylboronates from partially purified extracts of freshly dehisced tricellular pollen of rye-grass showed 25-methylcastasterone may be a minor component, together with two unknown peaks. No specific binding of brassinolide to any soluble proteins extracted from tricellular rye-grass pollen was observed using the antibodies in gel electrophoresis or enzyme-linked immunosorbent assays.
Language eng
Field of Research 059999 Environmental Sciences not elsewhere classified
Socio Economic Objective 970105 Expanding Knowledge in the Environmental Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Persistent URL http://hdl.handle.net/10536/DRO/DU:30039860

Document type: Journal Article
Collection: School of Life and Environmental Sciences
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