• Journal of Plant Biotechnology
• /
• v.30 no.4
• /
• pp.307-313
• /
• 2003

Fluorescent differential display (FDD) is a method for identifying differentially expressed genes in eukaryotic cells. The mRNA FDD technology works by systematic amplification of the 3' terminal regions of mRNAs. This method involve the reverse transcription using anchored primers designed to bind 5'boundary of the poly A tails, followed by polymerase chain reaction (PCR) amplification with additional upstream primers of arbitrary sequences. The amplified cDNA subpopulations are separated by denaturing polyacrylamide electrophoresis. To identify the genes involved in the development of first trap leaf, we applied a FDD method using mRNAs from leaf base, first trap leaf and flower tissue, respectively. We screened several genes that expressed specifically in first trap leaf. Nucleotide sequence analysis of these genes revealed that these were protease inhibitor (PI), myo-inositol-1-phosphate synthase and lipocalin-type prostaglandin D synthase. Northern blot analysis showed that these genes were expressed specifically in first trap leaf (in vivo and in vitro). FDD could prove to be useful for simultaneous scanning of transcripts from multiple cDNA samples and faster selection of differentially expressed transcripts of interest.

• Journal of the Microelectronics and Packaging Society
• /
• v.11 no.2 s.31
• /
• pp.37-41
• /
• 2004

Parallel combination of cold chathode fluorescent lamps (CCFL) are widely used as the light sources of LCD TV backlight. Brightness uniformity is safisfied by using one transformer per one CCFL. Instead of using one transformer per oneCCFL, one transformer is used to drive 8 CCFLs by using differential driving method. A differential driving inverter with two transformers is developed to drive 16 CCFLs of 26' backlight for LCD TV. The brightness uniformity of $88\%$ was obtained by driving 26' backlight with the developed differential driving inverter successfully.

• International Journal of Industrial Entomology and Biomaterials
• /
• v.13 no.1
• /
• pp.31-35
• /
• 2006

The ubiquitin conjugating enzyme 2 (E2) is core component of ubiquitin proteasome pathway (UPP) which represents a selective mechanism for intracellular proteolysis in eukaryotic cells. The E2 has been implicated in the intracellular transfer of ubiquitin to target protein. We show here the involvement of E2 in antiviral immune of Bombyx mori to Bombyx mori nuclear polyhedrosis virus (BmNPV). In this study, mRNA fluorescent differential display PCR (FDD-PCR) was performed with BmNPV highly resistant silkworm strain NB and susceptible silkworm strain 306. At 24 h post BmNPV infection, FDD-PCR with the arbitrary primer AP34 showed that one cDNA band was down-regulated in the midgut of resistant strain, but highly expressed in susceptible strain. The deduced amino acid sequence of this cDNA clone share 99% identity with the recently published B. mori ubiquitin conjugating enzyme E2 (Genbank NO: DQ311351). Fluorescent quantitative PCR corroborated down regulation of E2 in resistant strain. We there conclude that BmNPV infection evokes strong response of susceptible strain including activation of UPP. BmNPV may evolve escape mechanisms that manipulate the UPP in order to persist in the infected host. In addition, the identification of down-regulation of E2 in resistant strain, as well as structure data, are essential to understanding how UPP operates in silkworm antiviral immune to BmNPV disease.

• Proceedings of the Korean Society of Plant Biotechnology Conference
• /
• 2003.10a
• /
• pp.99-99
• /
• 2003