Storage protein profiles in Spanish and runner market type peanuts and potential markers

Liang, XQ; Luo, Meiying; Holbrook, C. C.; Guo, B. Z.

doi:10.1186/1471-2229-6-24

Cited by 49 publications

(32 citation statements)

References 27 publications

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“…In proteomic analysis of storage protein profiles in peanuts [12], total protein was extracted using a modified TCA/acetone precipitation protocol with the first step of de-fatting using hexane. Dry peanut kernels were frozen in liquid N 2 and ground to powder in a mill and defatted with hexane (10 mL/g dry weight) at -208C overnight.…”

Section: Legume Seedsmentioning

confidence: 99%

“…Examples of protein extraction from recalcitrant plant tissues for proteomic analysis Protein extraction protocols Species, tissues, and references TCA/acetone precipitation C. sativa roots [20], maize seeds [64] and roots [13], M. truncatula seeds [65] and roots [69], peanut seeds [12], olive seeds [66], soybean seed [68], wheat leaf [31], olive leaf [28], rice sheath [16] and internode [17], grape berry cluster [40] and mesocarp [72], fruits (banana, apple, strawberry) [38,39,61], potato tuber [71,73], woody tissue [74] Phenol extraction Maize roots [29], hemp roots [70], grape berry cluster [40], fruits (banana, apple, strawberry) [38,39,61], potato tuber [71] TCA/acetone/phenol extraction Leaves (olive, redwood, lemon, etc.) [27,34], posidonia leaf [50], fruits (apple, banana, grape, etc.)…”

Section: Grape Berriesmentioning

confidence: 99%

“…In recent years, such improvements in proteomics as high-resolution protein separation [4,5], MS software and hardware, and advanced bioinformatics technology [6,7], have led to an increasing application of proteomics in all biological fields, including functional plant studies [8 -11]. 2-DE combined with MS has proved to be the most powerful method for describing plant species and lines [12], protein identification in mixtures [13 -15], and stress responses [16 -20]. To date, several excellent reviews on plant proteomics have been published [8, 9, 21 -24].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Optimizing protein extraction from plant tissues for enhanced proteomics analysis

Wang¹,

Tai

Chen

2008

J of Separation Science

148

110

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Plant tissues usually contain high levels of proteases and secondary metabolites that severely interfere with protein extraction, separation, and identification. Preparation of high-quality protein samples from plant tissues for proteomic analysis represents a great challenge. This article briefly describes the critical points in protein separation, especially secondary metabolites in plant tissues, and removal strategy. It provides an updated overview of three total protein extraction methods and their applications in proteomic analysis of various recalcitrant tissues.

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Section: Legume Seedsmentioning

confidence: 99%

Section: Grape Berriesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Optimizing protein extraction from plant tissues for enhanced proteomics analysis

Wang¹,

Tai

Chen

2008

J of Separation Science

148

110

View full text Add to dashboard Cite

show abstract

“…The total protein extraction was modified from TCA/Acetone protein extraction protocol [16] with the first step being defatting using hexane as previously described [34]. Briefly, dry peanut kernels (20 g) of each genotype were frozen in liquid nitrogen and ground to powder and defatted with hexane (10 ml/g dry weight) at -20 o C overnight.…”

Section: Total Protein Extraction and 1-d And 2-d Electrophoresesmentioning

confidence: 99%

“…Among them are isozymes [51], restriction fragment length polymorphisms (RFLP), random amplified polymorphisms (RAPD), amplified fragment length polymorphisms (AFLP), and simple sequence repeats (SSR) [24][25][26]30]. Singh et al [48,49] and Bianchi-Hall et al [3] found very limited or no variation among cultivated peanut based on seed protein profiles, Liang et al [34] detected measurable variation between Spanish and runner type peanuts using two-dimensional (2-D) electrophoresis.…”

Section: Introductionmentioning

confidence: 99%

Proteomic Analysis of Peanut Seed Storage Proteins and Genetic Variation in a Potential Peanut Allergen

Guo¹,

Liang²,

Chung³

et al. 2008

PPL

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Peanut allergy is one of the most severe food allergies. One effort to alleviate this problem is to identify peanut germplasm with lower levels of allergens which could be used in conventional breeding to produce a less allergenic peanut cultivar. In this study, we identified one peanut line, GT-C9, lacking several seed proteins, which were identified as Ara h 3 isoforms by peptide sequencing and named iso-Ara h 3. Total seed proteins were analyzed by one-dimensional (SDS-PAGE) and two-dimensional gel electrophoreses (2-D PAGE). The total protein extracts were also tested for levels of protein-bound end products or adducts such as advanced glycation end products (AGE) and N-(carboxymethyl) lysine (CML), and IgE binding. Peanut genotypes of GT-C9 and GT-C20 exhibited significantly lower levels of AGE adducts and of IgE binding. This potential peanut allergen iso-Ara h 3 was confirmed by peptide sequences and Western blot analysis using specific anti-Ara h 1, Ara h 2, and Ara h 3 antibodies. A full-length sequence of iso-ara h 3 (GenBank number DQ855115) was obtained. The deduced amino acid sequence iso-Ara h 3 (ABI17154) has the first three of four IgE-binding epitopes of Ara h 3. Anti-Ara h 3 antibodies reacted with two groups of protein peptides, one with strong reactions and another with weak reactions. These peptide spots with weak reaction on 2-D PAGE to anti-Ara h 3 antibodies are subunits or isoallergens of this potential peanut allergen iso-Ara h 3. A recent study suggested that Ara h 3 basic subunits may be more significant allergenicity than the acidic subunits.

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2‐D DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents

et al. 2009

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Over the last decade, an increasing prevalence of peanut allergies was observed worldwide. Peanuts are meanwhile categorized among the most dangerous food allergens. This is particularly relevant since peanut-derived ingredients are widely used in industrial food production. To minimize the problem of hidden food allergens causing severe anaphylactic reactions, pre-packaged food containing peanut components needs to be classified according to European ruling since 2005. Food companies search for strategies to reduce the allergenicity of peanut-derived food additives either by genetically altering the allergen content or by identifying peanut varieties with low levels of major allergens. In our study, we focused on peanut extracts from Indonesia that apparently contain lower levels of the major Arachis hypogaea allergen 1 (Ara h 1). Basic extracts of Virginia-type and Indonesian peanuts were compared by 1- and 2-DE. We identified more than hundred individual components in these extracts by MS and provide a high-resolution allergen map that also includes so far unknown fragments of major peanut allergens. The reduced level of Ara h 1 associated with a significantly lower abundance of the most potent peanut allergen Ara h 2 in various Indonesian peanuts was also confirmed by Western blotting with monoclonal antibodies and sera of allergic patients.

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Storage protein profiles in Spanish and runner market type peanuts and potential markers

Cited by 49 publications

References 27 publications

Optimizing protein extraction from plant tissues for enhanced proteomics analysis

Optimizing protein extraction from plant tissues for enhanced proteomics analysis

Proteomic Analysis of Peanut Seed Storage Proteins and Genetic Variation in a Potential Peanut Allergen

2‐D DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents

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