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Database: PubMed
Entry: 9740056
LinkDB: 9740056
Original site: 9740056 
PMID:
     9740056
Authors:
     Tonella L, Walsh BJ, Sanchez JC, Ou K, Wilkins MR, Tyler M,
     Frutiger S, Gooley AA, Pescaru I, Appel RD, Yan JX, Bairoch A,
     Hoogland C, Morch FS, Hughes GJ, Williams KL, Hochstrasser DF.
Title:
     '98 Escherichia coli SWISS-2DPAGE database update.
Journal:
     Electrophoresis. 1998 Aug;19(11):1960-71.
Abstract:
     The combination of two-dimensional polyacrylamide gel electrophoresis (2-D PAGE),
     computer image analysis and several protein identification techniques allowed the
     Escherichia coli SWISS-2DPAGE database to be established. This is part of the
     ExPASy molecular biology server accessible through the WWW at the URL address
     http://www.expasy.ch/ch2d/ch2d-top.html . Here we report recent progress in the
     development of the E. coli SWISS-2DPAGE database. Proteins were separated with
     immobilized pH gradients in the first dimension and sodium dodecyl
     sulfate-polyacrylamide gel electrophoresis in the second dimension. To increase
     the resolution of the separation and thus the number of identified proteins, a
     variety of wide and narrow range immobilized pH gradients were used in the first 
     dimension. Micropreparative gels were electroblotted onto polyvinylidene
     difluoride membranes and spots were visualized by amido black staining. Protein
     identification techniques such as amino acid composition analysis, gel comparison
     and microsequencing were used, as well as a recently described Edman "sequence
     tag" approach. Some of the above identification techniques were coupled with
     database searching tools. Currently 231 polypeptides are identified on the E.
     coli SWISS-2DPAGE map: 64 have been identified by N-terminal microsequencing, 39 
     by amino acid composition, and 82 by sequence tag. Of 153 proteins putatively
     identified by gel comparison, 65 have been confirmed. Many proteins have been
     identified using more than one technique. Faster progress in the E. coli proteome
     project will now be possible with advances in biochemical methodology and with
     the completion of the entire E. coli genome.

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   UniProt (1)   
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