A two-dimensional protein map of Caenorhabditis elegans

Sabine P. Schrimpf; Hanno Langen; Ana Vaz Gomes; Claes R Wahlestedt

doi:10.1002/1522-2683()22:6<1224::AID-ELPS1224>3.0.CO;2-I

A two-dimensional protein map of Caenorhabditis elegans

Sabine P. Schrimpf, Hanno Langen, Ana Vaz Gomes, Claes R Wahlestedt

Research output: Contribution to journal › Article › peer-review

Abstract

A protein map of Caenorhabditis elegans was constructed by using two-dimensional gel electrophoresis followed by peptide mass fingerprinting. A whole worm extract of a mixed population was separated on immobilized pH gradient strips 4-7 L, 3-10 NL, 6-11 L and 12% sodium dodecyl sulfate-polyacrylamide gel eletrophoresis (SDS-PAGE) gels. Gels were stained with colloidal Coomassie blue and 286 spots representing 152 proteins were subsequently identified by matrix-assisted laser desorption/ionization-mass spectrometry after in-gel digestion with trypsin. Most of the identified proteins with known cellular function were enzymes related to carbohydrate and lipid metabolism, or structural proteins with subcellular locations in the cytoplasm, mitochondria or cytoskeleton.

Original language	English
Pages (from-to)	1224-1232
Number of pages	9
Journal	Electrophoresis
Volume	22
Issue number	6
DOIs	https://doi.org/10.1002/1522-2683()22:6<1224::AID-ELPS1224>3.0.CO;2-I
State	Published - May 17 2001
Externally published	Yes

Keywords

Caenorhabditis elegans
Peptide mass fingerprinting
Protein map
Two-dimensional gel electrophoresis

ASJC Scopus subject areas

Clinical Biochemistry

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AU - Langen, Hanno

AU - Gomes, Ana Vaz

AU - Wahlestedt, Claes R

PY - 2001/5/17

Y1 - 2001/5/17

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AB - A protein map of Caenorhabditis elegans was constructed by using two-dimensional gel electrophoresis followed by peptide mass fingerprinting. A whole worm extract of a mixed population was separated on immobilized pH gradient strips 4-7 L, 3-10 NL, 6-11 L and 12% sodium dodecyl sulfate-polyacrylamide gel eletrophoresis (SDS-PAGE) gels. Gels were stained with colloidal Coomassie blue and 286 spots representing 152 proteins were subsequently identified by matrix-assisted laser desorption/ionization-mass spectrometry after in-gel digestion with trypsin. Most of the identified proteins with known cellular function were enzymes related to carbohydrate and lipid metabolism, or structural proteins with subcellular locations in the cytoplasm, mitochondria or cytoskeleton.

KW - Caenorhabditis elegans

KW - Peptide mass fingerprinting

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A two-dimensional protein map of Caenorhabditis elegans

Abstract

Keywords

ASJC Scopus subject areas

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