Sub-cellular immunolocalization of the glucosinolate sinigrin in seedlings of Brassica juncea |
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Authors: | P J Kelly A Bones J T Rossiter |
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Institution: | (1) Department of Biological Sciences, Wye College, University of London, Wye, Ashford, Kent, TN25 5AH, UK, GB;(2) Unigen Center for Molecular Biology, Norwegian University for Science and Technology, MTFS, N-7005 Trondheim, Norway, NO |
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Abstract: | Polyclonal rat antibodies were raised to a bovine serum albumin-sinigrin conjugate and used to immunolocalize sinigrin (2-propenylglucosinolate)
in imbibed seeds and developing seedlings of Brassica juncea. (L.) Czern. Sinigrin was localized to protein bodies in aleurone-like cells but shown to be absent from myrosin cells. Double
labelling techniques were used to co-localize both myrosinase (β-thioglucoside glucohydrolase, EC 3.2.3.1) and sinigrin. Myrosin
grains were labelled only with the anti-myrosinase antibody, but aleurone cells were labelled with both anti-myrosinase and
anti-sinigrin antibodies. High-performance liquid chromatographic analysis of conventionally fixed and dehydrated seed tissues
(4 h post imbibition in water), indicated a high proportion of sinigrin was retained in fixed tissues. Over a time course
of 100 h, protein bodies within aleurone-like cells degraded, fused to form the cell vacuole and lost all myrosinase labelling
but retained residual sinigrin labelling. The degradation of protein bodies corresponded to a decrease in retention of sinigrin
in the fixed tissues. The results describe for the first time the co-localization of a plant enzyme and its substrate, a secondary
metabolite.
Received: 8 January 1998 / Accepted: 27 February 1998 |
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Keywords: | :Brassica (sinigrin immunolocalization) Glucosinolate Myrosinase Protein body β -Thioglucoside glucohydrolase |
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