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Hu S.,Sichuan Academy of Agricultural | Dong G.,Sichuan University | Chen X.,Sichuan University | Huang L.,Sichuan Academy of Agricultural | And 3 more authors.
Genetic Resources and Crop Evolution | Year: 2012

The internal transcribed spacer (ITS) region was employed to analyze phylogeny of 20 populations, including the local cultivar "Nanjiang", belonging to 7 species of Lonicera L. 20 ITS sequences that we obtained range from 614 to 618 bp, and the G+C content was higher than 60% with the average value 63.5%. The sequences of 5.8S nrDNA was highly conservative in both length and component, while ITS2 had more variation than ITS1 in sequence component and length. For the ITS complete sequence, the mutation and information sites were 139 and 117 with the content of 22.38 and 18.84%, respectively. The dendrogram analysed by neighbor-joining method showed that "Nanjiang" and Lonicera similis Hemsl. comprised a same cluster with a higher bootstrap support, indicating "Nanjiang" would be a variation or subspecies of L. similis Hemsl. The results of antibacterial activity test and active compounds identification showed that "Nanjiang" had the best antibacterial activity and the highest yield of chlorogenic acid, the active component of Flos Lonicerae, in the six species of Lonicera L. © 2011 Springer Science+Business Media B.V.

Liu B.,Sichuan University | Yao L.,Sichuan Academy of Agricultural | Wang W.,Sichuan University | Gao J.,Sichuan University | And 5 more authors.
Molecular Biology Reports | Year: 2010

Phospholipase D (PLD, EC is a key enzyme involved in phospholipid catabolism, initiating a lipolytic cascade in membrane deterioration during senescence and stress, which was cloned from Jatropha curcas L., an important plant species as its seed is the raw material for biodiesels. The cDNA was 2,886 bp in length with a complete open reading frame of 2,427 bp which encoded a polypeptide of 808 amino acids including a putative signal peptide of 53 amino acid residues and a mature protein of 755 amino acids with a predicted molecular mass of 86 kD and a pI of 5.44, having two highly conserved 'HKD' motifs. Phylogenetic analysis indicated the J. curcas PLD alpha (JcPLDa) showed a high similarity to other PLD alpha from plants. Semi-quantitative RT-PCR analysis revealed that it was especially abundant in root, stem, leaf, endosperm and flower, weakly in seed. And the JcPLDa was increasedly expressed in leaf undergoing environmental stress such as salt (300 mM NaCl), drought (30% PEG), cold (4°C) and heat (50°C). The JcPLDa protein was successfully expressed in Escherichia coli and showed high enzymatic activities. Maximal activity was at pH 8 and 60°C. © Springer Science+Business Media B.V. 2009.

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