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curcin/jarak pagar
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[Study on expression of curcin gene cloned from Jatropha curcas in Escherichia coli].
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OBJECTIVE
To construct mature protein curcin gene prokaryotic expression vectors in Escherichia coli and choose the optimal inducing condition of the recombinant strains.
METHODS
The gene encoding of curcin was amplified from the genome of Jatropha curcas seeds by PCR and cloned into the expression
RNAi Mediated curcin precursor gene silencing in Jatropha (Jatropha curcas L.).
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Curcin, a type I ribosomal inhibiting protein-RIP, encoded by curcin precursor gene, is a phytotoxin present in Jatropha (Jatropha curcas L.). Here, we report designing of RNAi construct for the curcin precursor gene and further its genetic transformation of Jatropha to reduce its transcript
Purification and characterization of curcin, a toxic lectin from the seed of Jatropha curcas.
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The seed of the plant Jatropha curcas contains a toxic protein, designated as curcin, which was purified to apparent homogeneity by the combined use of chromatography on Sephdex G-100. The molecular weight of 28.2 kDa and the pI of 8.54 were determined. The protein was found to be a glycoprotein;
Different functions and expression profiles of curcin and curcin-L in Jatropha curcas L.
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To date, two types of ribosome-inactivating proteins (RIPs) have been found in Jatropha curcas. One is curcin, which has been isolated from the endosperm, and the other is curcin-L, which is expressed in leaves upon stress treatment. Phylogenetic analysis of the predicted amino acid sequences of the
Analysis of seed phorbol-ester and curcin content together with genetic diversity in multiple provenances of Jatropha curcas L. from Madagascar and Mexico.
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Jatropha curcas L. has been promoted as an oilseed crop for use to meet the increased world demand for vegetable oil production, and in particular, as a feedstock for biodiesel production. Seed meal is a protein-rich by-product of vegetable oil extraction, which can either be used as an organic
Development of marker-free transgenic Jatropha curcas producing curcin-deficient seeds through endosperm-specific RNAi-mediated gene silencing.
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BACKGROUND
Jatropha curcas L. is a potential biofuel plant and its seed oil is suitable for biodiesel production. Despite this promising application, jatropha seeds contain two major toxic components, namely phorbol esters and curcins. These compounds would reduce commercial value of seed cake and
The effect of curcin from Jatropha curcas on apoptosis of mouse sarcoma-180 cells.
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Curcin is a ribosome-inactivating protein expressed in the endosperm of Jatropha curcas. Curcin can inhibit growth of mouse sarcoma-180 cells. At a curcin concentration of 100 μg/ml, mouse sarcoma-180 cell growth was inhibited by over 40% after seven days of incubation. Acridine orange staining and
Antitumor effects of curcin from seeds of Jatropha curcas.
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OBJECTIVE
To study the antitumor effects of curcin from Jatropha curcas.
METHODS
Antitumor activity of curcin was tested by MTT assay. The N-glycosidase activity of curcin was determined by characterization of R-fragment in gel. A cell-free system, rabbit reticulocyte lysate, was introduced to
Curcin C, a novel type I ribosome-inactivating protein from the post-germinating cotyledons of Jatropha curcas.
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A novel type I ribosome-inactivating protein (RIP), designated as curcin C, was purified from Jatropha curcas, an important feedback source of bio-fuel. Molecular mass and isoelectric point of curcin C were 31.398 kDa and 7.12 as detected by MALTI-TOF assay and capillary electrophoresis assay,
Expression of a ribosome inactivating protein (curcin 2) in Jatropha curcas is induced by stress.
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The open reading frame (ORF) encoding curcin 2 was cloned from total genomic and cDNA of Jatropha curcas leaves, which were treated by drought, temperature stress and fungal infection, by polymerase chain reaction (PCR) and reverse transcriptase (RT)-PCR amplification. The ORF has 927 bp that
Structure prediction and binding sites analysis of curcin protein of Jatropha curcas using computational approaches.
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Ribosome inactivating proteins (RIPs) are defense proteins in a number of higher-plant species that are directly targeted toward herbivores. Jatropha curcas is one of the biodiesel plants having RIPs. The Jatropha seed meal, after extraction of oil, is rich in curcin, a highly toxic RIP similar to
Stress-induced curcin-L promoter in leaves of Jatropha curcas L. and characterization in transgenic tobacco.
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Ribosome-inactivating proteins (RIPs) represent a type of protein that universally inactivates the ribosome thus inhibiting protein biosynthesis. Curcin-L was a type I RIP found in Jatropha curcas L.. Its expression could be activated in leaves by treatments with abscisic acid, salicylic acid,
Cloning and characterization of a curcin gene encoding a ribosome inactivating protein from Jatropha curcas.
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A curcin gene was isolated by using genomic walker technology and revealed to encode the type-1 ribosome inactivating proteins (RIPs). Analysis of 1802 bp segments revealed the gene including a 694 bp 5' flanking region, a 882 bp open read frame (ORF) and a 226 bp 3' flanking region. There are one
[Study of the toxicity and localization of toxalbumin (curcin) in the seeds of Jatropha curcas Linn].
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[Study of the proteins in the seeds of Jatropha curcas L. by means of solubility curves & localization of toxalbumin (curcin) on them].
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