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 | |
| State | Published - May 17 2001 |
| Externally published | Yes |
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Keywords
- Caenorhabditis elegans
- Peptide mass fingerprinting
- Protein map
- Two-dimensional gel electrophoresis
ASJC Scopus subject areas
- Clinical Biochemistry
Cite this
A two-dimensional protein map of Caenorhabditis elegans. / Schrimpf, Sabine P.; Langen, Hanno; Gomes, Ana Vaz; Wahlestedt, Claes R.
In: Electrophoresis, Vol. 22, No. 6, 17.05.2001, p. 1224-1232.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A two-dimensional protein map of Caenorhabditis elegans
AU - Schrimpf, Sabine P.
AU - Langen, Hanno
AU - Gomes, Ana Vaz
AU - Wahlestedt, Claes R
PY - 2001/5/17
Y1 - 2001/5/17
N2 - 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.
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
KW - Protein map
KW - Two-dimensional gel electrophoresis
UR - http://www.scopus.com/inward/record.url?scp=0035030137&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035030137&partnerID=8YFLogxK
U2 - 10.1002/1522-2683()22:6<1224::AID-ELPS1224>3.0.CO;2-I
DO - 10.1002/1522-2683()22:6<1224::AID-ELPS1224>3.0.CO;2-I
M3 - Article
VL - 22
SP - 1224
EP - 1232
JO - Electrophoresis
JF - Electrophoresis
SN - 0173-0835
IS - 6
ER -