CT findings of periappendiceal abscesses

Kang, Hee In; Kang, Kee Ryeon; Suh, Minseok; Lee, Y; Chung, S Y; Bae, Sang Hoon; Yoon, Jin-Han

doi:10.3348/jkrs.1987.23.2.277

Cited by 14 publications

(21 citation statements)

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“…After SDS-PAGE, the gel was stained by the colloidal Coomassie Brilliant Blue (CBB) staining method. 12) The staining solution consisted of 20% ethanol, 1 M ammonium nitrate, 20 mM phosphoric acid, and 0.08% CBB G-250. The gel was stained for 12-18 h and destained with distilled water until a clear background appeared.…”

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confidence: 99%

Separation and Identification of Rice Prolamins by Two-Dimensional Gel Electrophoresis and Amino Acid Sequencing

Shigemitsu

Saito

Morita

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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There are difficulties in detecting and separating rice prolamin polypeptides by 2D-PAGE analysis because prolamin polypeptides are insoluble, and the amino acid sequences show high homology among them. In this study, we improved the prolamin extraction method and the 2D-PAGE procedure, and succeeded in separating prolamin polypeptide species by 2D-PAGE and in identifying major prolamin polypeptide sequences.Key words: rice seed; prolamin; 2D-PAGE; amino acid sequencing Two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) is a powerful tool for the separation, quantification, and identification of proteins. Considerable research effort has been applied to the use of rice proteomic analysis to predict the functions of proteins, and much insight into the yield and quality of rice grain has been acquired. 1,2) Rice seed storage proteins consist mainly of glutelins and prolamins.3) 1D-PAGE analysis of prolamin polypeptides from isolated type I protein body (PB-I) indicated that PB-I contains 10 kDa, 13 kDa, and 16 kDa prolamins. 4) Two groups of 13 kDa prolamins have been defined: 13b prolamins were extracted in the absence of any reducing reagent, while the remaining 13a prolamins were extracted under reducing conditions similar to those used for the 10 kDa and 16 kDa prolamins. Several studies involving proteomic analysis of rice seed proteins have been reported, and albumins, globulins, and glutelins in rice seeds were well separated and identified by 2D-PAGE.5-7) However, little has been reported regarding the analysis of prolamins by 2D-PAGE. Recently, proteomic analysis of rice seeds by 2D-PAGE showed 400 protein spots, but only one spot was identified as a prolamin polypeptide.8) The reason is that the prolamins were less solubilized by a conventional lysis solution consisting of urea and non-ionic detergent for use in 2D-PAGE due to their hydrophobic property. There have been several advances recently in the methodologies of proteomic analysis, including improved protein extraction techniques.9,10) These studies indicate that a combination of urea, thiourea, and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS) was efficient for the extraction of highly insoluble proteins. These methods are expected to be useful in the extraction of prolamins from rice seeds. In addition, prolamin polypeptides are encoded by multi-gene families and have high homology. An NCBI database search indicated that there are three copies of 10 kDa prolamin, one copy of 16 kDa prolamin, four copies of 13a prolamin, and 13 copies of 13b prolamin. Due to this close sequence identity, it is difficult to separate prolamin polypeptides by isoelectric focusing (IEF)/SDS-PAGE. Hence we analyzed prolamin polypeptides by high-resolution nonequilibrium pH gradient gel electrophoresis (NEPHGE)/SDS-PAGE.11) In this study, we succeeded in detecting and separating several prolamin polypeptides by 2D-PAGE and in sequencing major prolamin polypeptides using an amino acid sequencer.Fifty mg of brown rice (Oryza sativa L. cv Nip...

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Separation and Identification of Rice Prolamins by Two-Dimensional Gel Electrophoresis and Amino Acid Sequencing

Shigemitsu

Saito

Morita

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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“…1,2 Among protein stains, dyes that bind non-covalently to protein-SDS complexes in SDS-PAGE are particularly useful for proteomic studies. 2,3 Unlike covalent binders that modify proteins permanently, they maintain chemical composition of proteins. Therefore, post-gel microanalysis, such as protein characterization using mass spectrometry, is not hampered by their presence.…”

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Hydrophobic Aminostyryl Quinolinium Dyes as New Fluorescent Stains for Proteins in Sodium Dodecyl Sulfate‐polyacrylamide Gel

et al. 2004

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“…SDS) and to achieve proper staining [41]. The fixation step is optional as the proteins are fixed and stained simultaneously by this CCB staining protocol [40]. Nonetheless, we strongly recommend the fixation step (2 h until overnight) to avoid loss of proteins during washing.…”

Section: Fixation (5) and Washing (6)mentioning

confidence: 99%

“…Hence, it is widely used for protein visualization. Several approaches have been made to enhance the limits of detection [40,[48][49][50][51][52]. The major drawback of this dye-based detection method is the unspecific background staining of the gel, which was identified as the major error source of quantitative GE [12,38].…”

Section: Ccb Staining (7) and Destaining (8)mentioning

confidence: 99%

Quantitative gel electrophoresis: New records in precision by elaborated staining and detection protocols

et al. 2011

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Gel electrophoresis (GE) is a very common analytical technique for proteome research and protein analysis. Despite being developed decades ago, there is still a considerable need to improve its precision. Using the fluorescence of Colloidal Coomassie Blue -stained proteins in near-infrared (NIR), the major error source caused by the unpredictable background staining is strongly reduced. This result was generalized for various types of detectors. Since GE is a multi-step procedure, standardization of every single step is required. After detailed analysis of all steps, the staining and destaining were identified as the major source of the remaining variation. By employing standardized protocols, pooled percent relative standard deviations of 1.2-3.1% for band intensities were achieved for one-dimensional separations in repetitive experiments. The analysis of variance suggests that the same batch of staining solution should be used for gels of one experimental series to minimize day-to-day variation and to obtain high precision.

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CT findings of periappendiceal abscesses

Cited by 14 publications

References 0 publications

Separation and Identification of Rice Prolamins by Two-Dimensional Gel Electrophoresis and Amino Acid Sequencing

Separation and Identification of Rice Prolamins by Two-Dimensional Gel Electrophoresis and Amino Acid Sequencing

Hydrophobic Aminostyryl Quinolinium Dyes as New Fluorescent Stains for Proteins in Sodium Dodecyl Sulfate‐polyacrylamide Gel

Quantitative gel electrophoresis: New records in precision by elaborated staining and detection protocols

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