jatropha pelargoniifolia/tyrosine

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Characterization, and expression profile of a phenylalanine ammonia lyase gene from Jatropha curcas L.

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A PAL gene designated as JcPAL1 was cloned from J. curcas L. The full-length is 2336 bp in size with one intron and two exons, encoding a polypeptide of 713 amino acids. Its 5'-upstream region is rich in putative cis-elements including not only PAL typical TATA box, L-box and transcriptional

Antioxidant and chelating activity of Jatropha curcas L. protein hydrolysates.

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BACKGROUND Antioxidant and chelating activities were determined in protein hydrolysates that were produced by treating a protein isolate of a non-toxic genotype of Jatropha curcas with the protease preparation alcalase. RESULTS 50 min protein hydrolysate with a degree of hydrolysis of 31.7% showed

Circular dichroism studies on the effects of sodium dodecyl sulfate on the conformation of some phytohemagglutinins.

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Conformation and conformational transitions of phytohemagglutinins (lectins) from Arachis hypogaea (peanut), Lens culinaris (lentil), Glycine max (soybean), and Ricinus communis (castor bean) were studied by the circular dichroism probe. The lectins were found to possess a high amount of the pleated

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

States of tryptophan residues in castor bean hemagglutinin: the perturbing effects of solvents on tryptophans in hemagglutinin and its complexes as analyzed by UV-difference spectroscopy.

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The states of tryptophan residues in castor bean hemagglutinin (CBH) were analyzed by solvent perturbation studies employing ultraviolet difference spectroscopy. Eight out of 22 tryptophan residues in CBH were exposed to ethylene glycol and glycerol, suggesting that the remaining 14 tryptophan

A role for SHPS-1/SIRPalpha in Concanavalin A-dependent production of MMP-9.

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SHPS-1/SIRPalpha1 is a transmembrane glycoprotein that belongs to the immunoglobulin (Ig) super family. In the present study, we show that SHPS-1 strongly associates with Concanavalin A (Con A), a plant lectin obtained from jack beans. Further studies with SHPS-1 mutants reveal that the

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