Glycoprotein detection of 2-D separated proteins

Nicolle H. Packer; Malcolm S. Ball; Peter L. Devine

doi:10.1385/1-59259-584-7:341

Glycoprotein detection of 2-D separated proteins

Nicolle H. Packer^*, Malcolm S. Ball, Peter L. Devine

^*Corresponding author for this work

Research output: Contribution to journal › Review article › peer-review

24 Citations (Scopus)

Abstract

The profile of the two-dimensional (2-D) separation of the protein complement (proteome) of eukaryotic cells and tissues typically contains obvious “trains” of spots that differ in pI and/or apparent molecular mass. These are usually isoforms of the same protein and result from a variety of posttranslational modifications. There is growing evidence that alterations to the glycosylation of a protein can be correlated with developmental and pathological changes; these changes can be visualized on the 2-D separation by alterations in the pattern of these glycoprotein isoforms.

Original language	English
Pages (from-to)	341-352
Number of pages	12
Journal	Methods in molecular biology (Clifton, N.J.)
Volume	112
DOIs	https://doi.org/10.1385/1-59259-584-7:341
Publication status	Published - 1999

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AB - The profile of the two-dimensional (2-D) separation of the protein complement (proteome) of eukaryotic cells and tissues typically contains obvious “trains” of spots that differ in pI and/or apparent molecular mass. These are usually isoforms of the same protein and result from a variety of posttranslational modifications. There is growing evidence that alterations to the glycosylation of a protein can be correlated with developmental and pathological changes; these changes can be visualized on the 2-D separation by alterations in the pattern of these glycoprotein isoforms.

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ER -

Glycoprotein detection of 2-D separated proteins

Abstract

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