All issues
Successor
Volume 49 (2005)
- Issue 4 Pages 97-
- Issue 3 Pages 63-
- Issue 2 Pages 31-
- Issue 1 Pages 1-
- Issue Supplement Page･･･
Volume 49, Issue 1
Displaying 1-3 of 3 articles from this issue
- |<
- <
- 1
- >
- >|
-
Takashi Morii, Takao Okada2005 Volume 49 Issue 1 Pages 1-3
Published: March 15, 2005
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSVisualization and measurement of biomolecules based on an atomic force microscope (AFM) allow us to observe individual molecules in their native form. Because the measurement can be performed in buffer solution and it does not require fluorescence labeling or staining. This technique could be applied for the detection of bound site of MutS protein to DNA successfully. Recent developments in AFM technology such as a low noise nano-positioning sensor for closed-loop operation have opened the door to new era of single molecule manipulation. We demonstrate that we can take aim at a portion of DNA adsorbed on mica substrate and we can fish it up with an AFM tip.View full abstractDownload PDF (4267K) -
Yoshitoshi Matsuda, Shogo Ebisu2005 Volume 49 Issue 1 Pages 5-9
Published: March 15, 2005
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe post-genomic era brings with it many challenges to the understanding of protein structure, function and interaction. The increasing number of newly identified proteins that need to be expressed, problems associated with cell cultivation, and traditional sub-cloning procedures are some of the key bottlenecks.
Rapid Translation System “RTS” is a scalable in vitro transcription/translation protein expression platform, that produces sufficient amounts of protein for characterization studies, functional assays, or structural analysis. RTS offers the advantages of a cell-free protein expression system, eliminating the need for laborious up- and down-stream steps (e.g. host cell transformation, culturing, or lysis) typically associated with cell-based expression systems.
Generally, to further fasten the protein expression screening, we recommend to use linear (PCR-generated) templates with the RTS screening kits. These templates are produced via the RTS Linear Template Generation Sets. For scale-up with RTS500 (1ml reaction) and RTS9000 (10, 30ml reaction), the use of circular templates is recommended, which are generated with the RTS pIVEX Vector Sets. In order to yield mg quantities, expressions should be performed using the RTS ProteoMaster instrument.
For optimization of the prokaryotic Rapid Translation, we offer a special software, the ProteoExpert RTS E. coli HY. The software delivers high-yield variants of an input ORF sequence.View full abstractDownload PDF (7599K) -
Etsuo Arai, Hiroshi Takai2005 Volume 49 Issue 1 Pages 11-16
Published: March 15, 2005
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe discovery stage of proteome profiling for disease or expression proteomics typically involves the comparison of different states of a cell, tissue or plasma. In order to obtain better reproducibility and quantitate proteins, 2-dimensional LC liquid separation technique, ProteomeLab PF2D is presented. This method uses chromatofocusing to produce pI fractionation in the first dimension, followed by RP chromatography in the second dimension to generate a 2-dimensional image of the protein content. The MALDI-TOF MS analysis of the second dimension fractions is also discussed.
Additionally, CE-ESI-MS utility in the protein identification and carbohydrate chain conformation analysis is presented. The triptic digested protein and the labeled oligosaccharides were elegantly analyzed by MS-MS. Also the labeled oligosaccharides analysis by CE system with laser-induced fluorescence detecting provided the additional information. The CE-ESI-MS technique complements LC-MS as a new powerful analytical tool for the fields of proteomics and glycomics to analyze the conformation of the N-linked oliosaccharides.View full abstractDownload PDF (6261K)
- |<
- <
- 1
- >
- >|