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Accession number;05A0323279
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| Title;Biochemistry. Identification of protein by a two-dimensional electrophoretic method. |
| Author;
MANABE TAKASHI
(Ehime Univ., Fac. Sci., JPN)
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Journal Title;Modern Medical Laboratory
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Journal Code:Z0084B
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ISSN:0301-2611
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VOL.33;NO.3;PAGE.235-240(2005)
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| Figure&Table&Reference;FIG.2, REF.1 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;The two-dimensional electrophoresis has been used as a high-performance separation method of protein since 1970's. As methods for identifying the protein that was separated in the two-dimensional electrophoresis, the following methods had been used, however, the efficiency enhancement was difficult in both methods : A method for dyeing immunochemically after electrophoretic transfer (blotting) of the protein pattern on the gel in a film such as nitrocellulose and a method for dyeing the protein after electrophoretic transfer on a film in a polyvinylide nefluoride (PVDF) film, and to cut out the specific spot part and afterwards, to decide amino acid sequence by Edman degradation. The mass spectrometry (MALDI (Matric assisted laser descorption ionization) - TOF (time of flight) MS (mass spectyrometry) and ESI - MS/MS) would be widely used since the latter half in 1990's as a method for identifying protein on the gel after two-dimensional electrophoresis. It seems that the use of mass spectrometry is the most efficient at present for the purpose to identify large number of protein spots which are separated in the two-dimensional electrophoresis simultaneously. |
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