jatropha ribifolia/proline

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Molecular cloning and expression analysis of the gene encoding proline dehydrogenase from Jatropha curcas L.

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Proline dehydrogenase (ProDH) (EC 1.5.99.8) is a key enzyme in the catabolism of proline. The enzyme JcProDH and its complementary DNA (cDNA) were isolated from Jatropha curcas L., an important woody oil plant used as a raw material for biodiesels. It has been classified as a member of the Pro_dh

[Effects of drought stress and nitrogen fertilization rate on the accumulation of osmolytes in Jatropha curcas seedlings].

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A pot experiment with controlled water supply was conducted to study the effects of different drought stress degree (80% FC, 60% FC, 40% FC, and 20% FC) and nitrogen fertilization rate (0 g x pot(-1), 1.2 g x pot(-1), 3.6 g x pot(-1), and 6.0 g x pot(-1)) on the accumulation of osmolytes in

Phytomonas: transport of amino acids, hexoses and polyamines.

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Phytomonas cells (Phytomonas Jma) isolated from the latex of Jatropha macrantha were assayed for amino acid, hexose and polyamine transport. Results showed high transport rates for glucose and fructose (193 and 128 pmol min(-1) 10(-7) cells, respectively) and lower, but significant rates, for

[Cytotoxic activity of two cyclic peptides from the latex of Jatropha integerrima Euphorbiaceae].

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Activity-guided fractionation of the ethyl acetate extract of the latex of Jatropha integerrima Euphorbiaceae combinated with cytotoxic assay against the KB human nasopharyngeal carcinoma cells, resulted to the isolation by chromatographic methods including HPLC of two new cyclopeptides:

A New AP2/ERF Transcription Factor from the Oil Plant Jatropha curcas Confers Salt and Drought Tolerance to Transgenic Tobacco.

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Jatropha curcas L. is a drought and salt-tolerant oil plant widely used for various purposes and has considerable potential as a diesel/kerosene substitute or extender. Understanding the molecular mechanisms underlie that the response to various biotic and abiotic stresses of this plant could be

Primary structure of the major allergen of yellow mustard (Sinapis alba L.) seed, Sin a I.

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Sin a I, a 2-S albumin from the seeds of yellow mustard, is herein described as the major allergen of these seeds. This protein is composed of two disulfide-linked polypeptide chains of 39 and 88 amino acids, whose primary structures are reported. The Sin a I allergen is found to be related to other

Jatropha curcas oil body proteome and oleosins: L-form JcOle3 as a potential phylogenetic marker.

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The seed oil of Jatropha curcas has been proposed as a source of biodiesel. In plants, seed oil is stored in subcellular organelles called oil bodies (OBs), which are stabilized by proteins. Proteome composition of the J. curcas OBs revealed oleosins as the major component and additional proteins

Computational identification and phylogenetic analysis of the oil-body structural proteins, oleosin and caleosin, in castor bean and flax.

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Oil bodies (OBs) are the intracellular particles derived from oilseeds. These OBs store lipids as a carbon resource, and have been exploited for a variety of industrial applications including biofuels. Oleosin and caleosin are the common OB structural proteins which are enabling biotechnological

Ricinus communis L. (castor bean) as a potential candidate for revegetating industrial waste contaminated sites in peri-urban Greater Hyderabad: remarks on seed oil.

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Ricinus communis L. (castor bean or castor oil plant) was found growing on metal-contaminated sites (4) of peri-urban Greater Hyderabad comprises of erstwhile industrial areas viz Bollaram, Patancheru, Bharatnagar, and Kattedan industrial areas. During 2013-2017, about 60 research papers have

Proteases and Peptidases of Castor Bean Endosperm: Enzyme Characterization and Changes during Germination.

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The endosperm of castor bean seeds (Ricinus communis L.) contains two -SH-dependent aminopeptidases, one hydrolyzing l-leucine-beta-naphthylamide optimally at pH 7.0, and the other hydrolyzing l-proline-beta-naphthylamide optimally at pH 7.5. After germination the endosperm contains in addition an

Amino acid sequence of small and large subunits of seed storage protein from Ricinus communis.

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The low molecular weight, glutamine-rich storage protein isolated from the seeds of Ricinus communis (castor beans) has been shown to consist of two different polypeptide chains linked by disulfide bond(s). The small subunit is composed of 34 amino acids with a proline at its NH2 terminus, whereas

Isolation and partial characterization of antigen 5.1 from the seeds of Ricinus communis, L. (Var. Amarelo de Irece).

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Antigen 5.1 was isolated from the most acidic fraction of castor bean allergens (CB-1A) by gel filtration on Sephadex G-75 followed by polyacrylamide gel electrophoresis (PAGE) (yield: 6.2 mg antigen 5.1/g CB-1A). This antigen was homogeneous by the criteria of PAGE, isoelectric focusing, SDS-PAGE,

Characterization of Ricinus communis phloem profilin, RcPRO1.

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The mature, functional sieve tube, which forms the conduit for assimilate distribution in higher plants, is dependent upon protein import from the companion cells for maintenance of the phloem long-distance translocation system. Using antibodies raised against proteins present in the sieve-tube

Ex vivo processing for maturation of Arabidopsis KDEL-tailed cysteine endopeptidase 2 (AtCEP2) pro-enzyme and its storage in endoplasmic reticulum derived organelles.

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Ricinosomes are specialized ER-derived organelles that store the inactive pro-forms of KDEL-tailed cysteine endopeptidases (KDEL-CysEP) associated with programmed cell death (PCD). The Arabidopsis genome encodes three KDEL-CysEP (AtCEP1, AtCEP2, and AtCEP3) that are differentially expressed in

Pollinosis to Ricinus communis (castor bean): an aerobiological, clinical and immunochemical study.

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BACKGROUND Ricinus communis (castor bean) is a species included into the Euphorbiaceae family, common to all the warm regions of the world. Although the allergenicity of its seed is well known, references are scarce regarding the role played by its pollen as a pneumo-allergen. OBJECTIVE To carry out

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