jatropha ribifolia/albumiin

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A new 2S albumin from Jatropha curcas L. seeds and assessment of its allergenic properties.

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Significant effort has been made world-wide to boost biofuels with the expectation of a positive contribution to renewable fuel and greenhouse gas reduction. Jatropha curcas L. has proved to be an opportunistic crop in tropical areas, particularly in unfavorable environments. For this reason,

Sequence-specific, Golgi-dependent vacuolar targeting of castor bean 2S albumin.

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The targeting of the castor bean (Ricinus communis) 2S albumin precursor has been investigated by expressing cDNA in transformed tobacco (Nicotiana tabacum) leaf cells and by following biosynthesis in the native tissue. Correct targeting in both tissues was accompanied by processing of the

Albumin storage proteins in the protein bodies of castor bean.

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Of the total protein in the protein bodies of castor bean (Ricinus communis L.), approximately 40% is represented by a group of closely related albumins localized in the matrix of the organelle. This group of albumins has a sedimentation value of 2S and is resolved into several proteins of molecular

The Ricinus communis 2S albumin precursor: a single preproprotein may be processed into two different heterodimeric storage proteins.

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The Ricinus communis (castor bean) 2S albumin is a heterodimer of glutamine-rich, disulphide-linked 4 and 7 kDa polypeptide. A cDNA library was constructed using mRNA from maturing castor bean endosperm as template. Clones containing sequences complementary to albumin mRNA were isolated by

Transport of ricin and 2S albumin precursors to the storage vacuoles of Ricinus communis endosperm involves the Golgi and VSR-like receptors.

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We have studied the transport of proricin and pro2S albumin to the protein storage vacuoles of developing castor bean (Ricinus communis L.) endosperm. Immunoelectron microscopy and cell fractionation reveal that both proteins travel through the Golgi apparatus and co-localize throughout their route

Characterization and sequence of tomato 2S seed albumin: a storage protein with sequence similarities to the fruit lectin.

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We found a 2S storage albumin from the seed of tomato ( Lycopersicon esculentum L. cv. Cherry) that cross-reacted with antiserum to the fruit lectin, and named it Lec2SA. According to its size and basicity, Lec2SA was classified into four isoforms. These isoforms have an M(r) of approximately

Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis.

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The three-dimensional structure in aqueous solution of recombinant (15)N labeled RicC3, a 2S albumin protein from the seeds of castor bean (Ricinus communis), has been determined by NMR methods. The computed structures were based on 1564 upper limit distance constraints derived from NOE

Solution structure of a methionine-rich 2S albumin from sunflower seeds: relationship to its allergenic and emulsifying properties.

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The three-dimensional structure in aqueous solution of SFA-8, a 2S albumin 103-residue protein from seeds of sunflower (Helianthus anuus L.), has been determined by NMR methods. An almost complete (1)H resonance assignment was accomplished from analysis of two-dimensional (2D) COSY and 2D TOCSY

Evidence that the castor bean allergens are the albumin storage proteins in the protein bodies of castor bean.

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The well characterized castor bean (Ricinus communis L.) allergens were identified as the low molecular weight albumin storage proteins in the matrix of the protein bodies in the endosperm. The methods of identification involved molecular weight estimation, amino acid composition, stability at 100

Jatropha curcas hemagglutinin is similar to a 2S albumin allergen from the same source and has unique sugar affinities.

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We have previously reported the purification and preliminary X-ray characterization of a hemagglutinin from the seeds of Jatropha curcas and, with the detailed sequencing information available now, we find that it is similar to a 2S albumin allergen isolated from the same source. Through a search of

Isolation of phytate from Jatropha curcas kernel meal and effects of isolated phytate on growth, digestive physiology and metabolic changes in Nile tilapia (Oreochromis niloticus L.).

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Jatropha curcas seeds are rich in oil and protein. The oil is used for biodiesel production. The defatted Jatropha kernel meal obtained after oil extraction is rich in protein (58-66%) and phytate (9-11%). The phytate rich fraction was isolated from defatted kernel meal using organic solvents

Comparative nutritional value of Jatropha curcas protein isolate and soy protein isolate in common carp.

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Jatropha seed cake (JSC) is an excellent source of protein but does contain some antinutritional factors (ANF) that can act as toxins and thus negatively affect the growth and health status of fish. While this can limit the use of JSC, detoxified Jatropha protein isolate (DJPI) may be a better

Identification of IgE-binding peptide and critical amino acids of Jatropha curcas allergen involved in allergenic response.

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Increasing energy demand has spurred interest in the use of biofuels. Jatropha curcas (physic nut), an inedible oilseed, is a potential source of bioenergy. The seeds, however, contain allergens such as Jat c 1, a 2S albumin that can induce hypersensitivity reactions in humans and result in allergic

Molecular cloning of cDNA, recombinant protein expression and characterization of a buckwheat 16-kDa major allergen.

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BACKGROUND Buckwheat is a common food in Japan, Korea and other countries. A candidate major buckwheat allergen, a 16-kDa protein (BWp16), was previously characterized as a pepsin-resistant protein associated with immediate-type allergies to buckwheat. However, whether recombinant BWp16 can react

Immunological characterization and mutational analysis of the recombinant protein BWp16, a major allergen in buckwheat.

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Buckwheat allergy is one of the most critical diseases manifested by severe and dangerous symptoms in Japan and other countries. We previously isolated the cDNA encoding protein BWp16, a member of the 2S albumin family with a conserved motif of 8 cysteine (Cys) residues. Comparison of the deduced

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