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lupinus arboreus/albumine
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Identification and characterisation of the IgE-binding proteins 2S albumin and conglutin gamma in almond (Prunus dulcis) seeds.
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BACKGROUND
Almond proteins can cause severe anaphylactic reactions in susceptible individuals. The aim of this study was the identification of IgE-binding proteins in almonds and the characterisation of these proteins by N-terminal sequencing.
METHODS
Five sera were selected from individuals with a
Some 2S albumin from peanut seeds exhibits inhibitory activity against Aspergillus flavus.
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A crude 2S albumin fraction was separated from peanut (Arachis hypogaea L.) cotyledons. Untreated 2S albumin had little inhibitory activity against trypsin, spore germination, or hyphal growth of Aspergillus flavus. However, following treatment of 2S albumin with SDS, increased inhibitory activity
Enhanced methionine levels and increased nutritive value of seeds of transgenic lupins (Lupinus angustifolius L.) expressing a sunflower seed albumin gene.
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With the aim of improving the nutritive value of an important grain legume crop, a chimeric gene specifying seed-specific expression of a sulfur-rich, sunflower seed albumin was stably transformed into narrow-leafed lupin (Lupinus angustifolius L.). Sunflower seed albumin accounted for 5% of
Capillary electrophoresis of seed 2S albumins from Lupinus species.
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Two modes of capillary electrophoresis (CE)--free-solution capillary zone electrophoresis (CZE) and sodium dodecyl sulfate capillary electrophoresis (SDS-CE) using a non-gel sieving matrix--have been developed for comparative analysis of low-molecular-mass 2S albumin isoforms from lupins. The
Characterisation of a developmentally related polypeptide with glutelin solubility characteristics from Lupinus albus L.
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Proteins from Lupinus albus L. cv. Rio Maior seeds were fractionated according to solubility criteria. Patterns of concanavalin A (ConA)-binding polypeptides from the different classes, albumins, globulins, glutelins and prolamins, were established by sodium dodecyl sulfate-polyacrylamide gel
Storage proteins from Lathyrus sativus seeds.
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The proteins from Lathyrus sativus Linn. (chickling vetch or grass pea) seeds were investigated. Protein constitutes approximately 20% of the seed dry weight, >60% of which is composed by globulins and 30% by albumins. A single, 24 kDa polypeptide comprises more than half of the protein present in
Isolation and foaming functionality of acid-soluble protein from lupin (Lupinus angustifolius) kernels.
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BACKGROUND
Australian sweet lupin (ASL) protein is conventionally isolated by alkaline extraction/acid precipitation, leaving a waste stream containing acid-soluble proteins (ASPs) and contaminating raffinose family oligosaccharides (RFOs). The foaming functionality of ASP isolated from ASL is not
Monoclonal antibodies against the candidate lupin allergens alpha-conglutin and beta-conglutin.
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BACKGROUND
The ingestion of dietary products containing sweet lupin (such as Lupinus albus or Lupinus angustifolius) has been reported to cause IgE-mediated allergic reactions. Recent studies have indicated lupin globulins as important IgE binding proteins. The aim of the present study was to
[Sweet lupine (Lupinus luteus, var. Aurea/Weico and Lupinus albus, var. Multolupa) proteins. I. Extraction and filtration by Sephadex].
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Samples of Lupinus luteus, var. Aurea/Weico and Lupinus albus var. Multolupa flours were analyzed. The flour proteins were extracted and fractionated by gel filtration, and the per cent pattern for both globulins and albumins was then determined. The dehulled seeds, previously analyzed for
[Sweet lupine (Lupinus luteus, var. Aurea/Weico and Lupinus albus, var. Multolupa) proteins. II. Separation by electrophoresis].
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The albumins and globulins extracted from Lupinus luteus var. Aurea/Weico and Lupinus albus var. Multolupa defatted flour samples were analyzed by polyacrilamide gel electrophoresis. The purpose was to determine the percentage distribution of pattern in the electrophoretograms and the relative
Emulsifying and Foaming Properties of Different Protein Fractions Obtained from a Novel Lupin Variety AluProt-CGNA(®) (Lupinus luteus).
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The use of vegetable proteins as food ingredient is becoming increasingly important due to their high versatility and environmental acceptability. This work describes a chemical characterization and techno-functional properties (emulsifying and foaming properties) of 3 protein fractions obtained
Identification and characterisation of seed storage protein transcripts from Lupinus angustifolius.
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BACKGROUND
In legumes, seed storage proteins are important for the developing seedling and are an important source of protein for humans and animals. Lupinus angustifolius (L.), also known as narrow-leaf lupin (NLL) is a grain legume crop that is gaining recognition as a potential human health food
A plant-based allergy vaccine suppresses experimental asthma via an IFN-gamma and CD4+CD45RBlow T cell-dependent mechanism.
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Allergic asthma is currently considered a chronic airway inflammatory disorder associated with the presence of activated CD4(+) Th2-type lymphocytes, eosinophils, and mast cells. Interestingly, therapeutic strategies based on immune deviation and suppression have been shown to successfully attenuate
Protein distribution in lupin protein isolates from Lupinus angustifolius L. prepared by various isolation techniques.
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Differences in the protein distribution of various protein isolates from Lupinus angustifolius L. Vitabor were identified as affected by the isolation procedure (alkaline and/or salt-induced extraction followed by isoelectric and/or dilutive precipitation). Protein isolates extracted in alkaline
Lupin protein influences the expression of hepatic genes involved in fatty acid synthesis and triacylglycerol hydrolysis of adult rats.
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To assess the effect of lupin protein on concentrations of lipids in plasma lipoproteins and liver and hepatic mRNA concentrations of genes involved in lipid metabolism, adult rats were fed egg albumin-based diets containing either lupin protein from Lupinus albus or casein (50 g/kg) supplemented
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