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

Access to Document

10.1385/1-59259-584-7:341

Cite this

@article{e031e8bd346a48d191045d359a9e34c0,

title = "Glycoprotein detection of 2-D separated proteins",

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.",

author = "Packer, {Nicolle H.} and Ball, {Malcolm S.} and Devine, {Peter L.}",

year = "1999",

doi = "10.1385/1-59259-584-7:341",

language = "English",

volume = "112",

pages = "341--352",

journal = "Methods in molecular biology (Clifton, N.J.)",

issn = "1064-3745",

publisher = "Humana Press",

}

TY - JOUR

T1 - Glycoprotein detection of 2-D separated proteins

AU - Packer, Nicolle H.

AU - Ball, Malcolm S.

AU - Devine, Peter L.

PY - 1999

Y1 - 1999

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=0032605344&partnerID=8YFLogxK

U2 - 10.1385/1-59259-584-7:341

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

M3 - Review article

C2 - 10027260

AN - SCOPUS:0032605344

VL - 112

SP - 341

EP - 352

JO - Methods in molecular biology (Clifton, N.J.)

JF - Methods in molecular biology (Clifton, N.J.)

SN - 1064-3745

ER -

Glycoprotein detection of 2-D separated proteins

Abstract

Access to Document

Other files and links

Fingerprint

Cite this