中国生物工程杂志

Tapping panel dryness (TPD) occurrence in high latex yielding rubber tree (Hevea brasiliensis) is characterized by the partial or complete cessation of latex flow upon tapping leading to severe loss in natural rubber production around the world. To better explore and understand the mechanism of Tapping Panel Dryness(TPD) of Hevea brasiliensis onset, differential proteomic analysis is conducted in C-serum proteins from latex of healthy and TPD trees by two-dimension gel electrophoresis (2-DE) .The C-serum proteins from latex of healthy and TPD trees were separated by immobilized pH gradient(IPG) based 2-DE. The commassie brilliant blue-stained 2-DE were scanned with digital Image Scanner and analyzed with PDQuest 7.40 analysis software. After in-gel protein digestion , peptide mass fingerprint ( PMF) of different-expressed protein spots were obtained with matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and database searching were used to identify proteins in Swiss-Prot and NCBInr database by Mascot software. Results:　①Average protein spots were 1075±35, 1134±27 in C-serum proteins from latex of healthy and TPD respectively, the matched spots were 982±38,1008±22 in both the two types of tissues respectively , and the average matching rate was 91.89﹪,88.72﹪ respectively. ②A total of 970±25 protein spots was matched between the 2-DE map of C-serum proteins from latex of healthy and TPD. Forty spots with changed expression level remarkably were measured by MALDI- TOF-MS and 27 proteins were identified. In this study, the well-resolved and reproducible 2-DE patterns of C-serum proteome from latex of healthy and TPD trees were established and some different-expressed protein spots between the two types of tissues were detected by mass spectrometry. These proteins may be involved the onset of TPD syndrome. The results presented here demonstrate that 2-DE technique provides a powerful complementary approach for the identification of TPD related proteins from rubber tree.