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1                                              2D-PAGE followed by mass spectrometry identified 527 pro
2                                              2D-PAGE images showed that proteins in the biocake (S3)
3 PLC (fast protein liquid chromatography) and 2D-PAGE (two-dimensional polyacrylamide gel electrophore
4 d medium rare prepared beef were assessed by 2D PAGE for the comparison of protein profiles.
5 ver, separated by RP-HPLC, and identified by 2D PAGE techniques and immunoblotting.
6 for formation of such dimers was obtained by 2D PAGE of extracts of cells treated with inducers, and
7 s measured by qPCR but was not identified by 2D-PAGE.
8 icacy in separating soybean seed proteins by 2D-PAGE.
9 seed storage proteins were well separated by 2D-PAGE with minor variations in the intensity of the sp
10 ensional polyacrylamide gel electrophoresis (2D PAGE), we identified two specific proteins in skeleta
11 ensional polyacrylamide gel electrophoresis (2D-PAGE) and mass spectrometry analysis is challenging a
12 ensional polyacrylamide gel electrophoresis (2D-PAGE) and phospho-specific flow cytometry.
13 ensional polyacrylamide gel electrophoresis (2D-PAGE) and shotgun proteomics (1D-PAGE-liquid chromato
14 ensional polyacrylamide gel electrophoresis (2D-PAGE) and tandem mass spectrometry to characterize th
15 ensional polyacrylamide gel electrophoresis (2D-PAGE) is the common method of choice for proteomic an
16 ensional polyacrylamide gel electrophoresis (2D-PAGE) of retinal protein lysates obtained from eyes m
17 ensional polyacrylamide gel electrophoresis (2D-PAGE) separation and matrix-assisted laser desorption
18 mensional polyacrylmide gel electrophoresis (2D-PAGE), perhaps the most widely used method in proteom
19 ensional polyacrylamide gel electrophoresis (2D-PAGE).
20 ensional polyacrylamide gel electrophoresis (2D-PAGE).
21 ndance proteins and is a suitable method for 2D-PAGE separation and identification.
22 m genome and experimental data obtained from 2D-PAGE.
23  microsequencing, immunochemical analysis of 2D-PAGE blots and size exclusion chromatography indicate
24                                  Analysis of 2D-PAGE showed that proteins which were less abundant or
25 proved the resolution and reproducibility of 2D-PAGE but also shortened the time of analysis.
26     Only 169 proteins were identified by the 2D-PAGE and shotgun methods, which highlights the advant
27 ll extracts into well-defined pools prior to 2D PAGE on a scale directly compatible with the high sen
28 own to provide a liquid-based alternative to 2D-PAGE for intact protein profiling.
29  (MS) provides a liquid-based alternative to 2D-PAGE that can overcome these problems but is limited
30                                        Using 2D-PAGE, we demonstrate that mutant alpha-tropomyosinslo

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