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자료유형
학술저널
저자정보
Jeon, Yul-Taek (Department of Agricultural Biotechnology and Research Institute of Agricultural Sciences, Seoul National University) Ruzicka, Margaret R. (Department of Molecular Bioscience and Bioengineering, University of Hawaii) Cho, Il-Kyu (Department of Molecular Bioscience and Bioengineering, University of Hawaii) Li, Qing Xiao (Department of Molecular Bioscience and Bioengineering, University of Hawaii) Kim, Soo-Un (Department of Agricultural Biotechnology and Research Institute of Agricultural Sciences, Seoul National University)
저널정보
한국응용생명화학회 Applied Biological Chemistry Applied Biological Chemistry 제54권 제1호
발행연도
2011.1
수록면
19 - 23 (5page)

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Though urea helps solubilize the protein samples, use of urea under the boiling condition is generally avoided due to carbamylation of protein by cyanate in equilibrium with urea. Validity of adding urea in standard sample buffer and subjecting the standard protein, bovine serum albumin, to SDS-PAGE according to Laemmli procedure, which invariably involves heating of the protein sample at $100^{\circ}C$, was evaluated. Heating samples with crystalline ultra-pure urea improved separation, and the peptide mass fingerprint of the gel-separated protein by matrixassisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometer (MALDI TOF/TOF MS) indicated that the protein could be identified without difficulty with 39.2% of peptide coverage, which was comparable to the value obtained from the protein not treated with urea.

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