Electrospray MS and MALDI imaging show that non‐specific lipid‐transfer proteins (LTPs) in tomato are present as several isoforms and are concentrated in seeds. (December 2014)
- Record Type:
- Journal Article
- Title:
- Electrospray MS and MALDI imaging show that non‐specific lipid‐transfer proteins (LTPs) in tomato are present as several isoforms and are concentrated in seeds. (December 2014)
- Main Title:
- Electrospray MS and MALDI imaging show that non‐specific lipid‐transfer proteins (LTPs) in tomato are present as several isoforms and are concentrated in seeds
- Authors:
- Bencivenni, Mariangela
Faccini, Andrea
Zecchi, Riccardo
Boscaro, Francesca
Moneti, Gloriano
Dossena, Arnaldo
Sforza, Stefano - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Non‐specific lipid‐transfer proteins (nsLTPs) are major human allergens in many plant species, albeit their role in plant biochemistry is still undefined. They are found in many plant species, either as one or several isoforms according to the species, and usually they are found to concentrate in the outer part of the fruits. In this work, the characterization of tomato nsLTP isoforms was performed on the three main fractions of Piccadilly tomato fruit (peel, pulp and seeds) by using ultracentrifuge devices with molecular cut‐off able to retain proteins with molecular weight typical of plant LTPs. The isolated proteins were further analysed by LC‐MS, in order to investigate the occurrence and the localization of tomato LTP isoforms. The chromatographic retention times, the molecular masses, the presence of eight cysteine residues in their tertiary structures and the sequence information obtained by MS, although not complete yet, allowed us to identify four different LTP isoforms, not yet reported in the literature, which were found to be concentrated in the seed fractions. None of the molecular masses of these potential LTPs was already present in the UniProtKB/SwissProt database. MALDI imaging experiments confirmed their presence and main localization in seeds, although the actual data hinted at their presence around seeds, rather than exactly in them. These data hint to a complicated<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Non‐specific lipid‐transfer proteins (nsLTPs) are major human allergens in many plant species, albeit their role in plant biochemistry is still undefined. They are found in many plant species, either as one or several isoforms according to the species, and usually they are found to concentrate in the outer part of the fruits. In this work, the characterization of tomato nsLTP isoforms was performed on the three main fractions of Piccadilly tomato fruit (peel, pulp and seeds) by using ultracentrifuge devices with molecular cut‐off able to retain proteins with molecular weight typical of plant LTPs. The isolated proteins were further analysed by LC‐MS, in order to investigate the occurrence and the localization of tomato LTP isoforms. The chromatographic retention times, the molecular masses, the presence of eight cysteine residues in their tertiary structures and the sequence information obtained by MS, although not complete yet, allowed us to identify four different LTP isoforms, not yet reported in the literature, which were found to be concentrated in the seed fractions. None of the molecular masses of these potential LTPs was already present in the UniProtKB/SwissProt database. MALDI imaging experiments confirmed their presence and main localization in seeds, although the actual data hinted at their presence around seeds, rather than exactly in them. These data hint to a complicated scenario concerning LTP proteins in tomato. Copyright © 2014 John Wiley &amp; Sons, Ltd.</p> </abstract> … (more)
- Is Part Of:
- Journal of mass spectrometry. Volume 49:Number 12(2014:Dec.)
- Journal:
- Journal of mass spectrometry
- Issue:
- Volume 49:Number 12(2014:Dec.)
- Issue Display:
- Volume 49, Issue 12 (2014)
- Year:
- 2014
- Volume:
- 49
- Issue:
- 12
- Issue Sort Value:
- 2014-0049-0012-0000
- Page Start:
- 1264
- Page End:
- 1271
- Publication Date:
- 2014-12
- Subjects:
- Mass spectrometry -- Periodicals
543.65 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
- DOI:
- 10.1002/jms.3454 ↗
- Languages:
- English
- ISSNs:
- 1076-5174
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5012.179500
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3744.xml