Abstract
The rate of protein digestion imposes significant limitations on high-throughput protein identification using mass spectrometry. In this report, we demonstrate that proteins are readily digested by trypsin in the presence of organic solvents such as methanol, acetone, 2-propanol, and acetonitrile. The rates of protein digestion in organic solvents, as indicated by the abundances of digest fragment ions in the mass spectrum, are increased relative to aqueous solution. In addition, amino acid coverage for the analyzed proteins increases in the presence of the organic solvents, and proteins that are resistant to proteolysis are readily digested. For example, a 68% amino acid sequence coverage was attained from a tryptic digest of myoglobin in
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2682-2685 |
| Number of pages | 4 |
| Journal | Analytical Chemistry |
| Volume | 73 |
| Issue number | 11 |
| DOIs | |
| State | Published - Jun 1 2001 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Analytical Chemistry
Cite this
Proteolysis in mixed organic-aqueous solvent systems : Applications for peptide mass mapping using mass spectrometry. / Russell, William; Park, Z. Y.; Russell, D. H.
In: Analytical Chemistry, Vol. 73, No. 11, 01.06.2001, p. 2682-2685.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Proteolysis in mixed organic-aqueous solvent systems
T2 - Applications for peptide mass mapping using mass spectrometry
AU - Russell, William
AU - Park, Z. Y.
AU - Russell, D. H.
PY - 2001/6/1
Y1 - 2001/6/1
N2 - The rate of protein digestion imposes significant limitations on high-throughput protein identification using mass spectrometry. In this report, we demonstrate that proteins are readily digested by trypsin in the presence of organic solvents such as methanol, acetone, 2-propanol, and acetonitrile. The rates of protein digestion in organic solvents, as indicated by the abundances of digest fragment ions in the mass spectrum, are increased relative to aqueous solution. In addition, amino acid coverage for the analyzed proteins increases in the presence of the organic solvents, and proteins that are resistant to proteolysis are readily digested. For example, a 68% amino acid sequence coverage was attained from a tryptic digest of myoglobin in
AB - The rate of protein digestion imposes significant limitations on high-throughput protein identification using mass spectrometry. In this report, we demonstrate that proteins are readily digested by trypsin in the presence of organic solvents such as methanol, acetone, 2-propanol, and acetonitrile. The rates of protein digestion in organic solvents, as indicated by the abundances of digest fragment ions in the mass spectrum, are increased relative to aqueous solution. In addition, amino acid coverage for the analyzed proteins increases in the presence of the organic solvents, and proteins that are resistant to proteolysis are readily digested. For example, a 68% amino acid sequence coverage was attained from a tryptic digest of myoglobin in
UR - http://www.scopus.com/inward/record.url?scp=0035356739&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035356739&partnerID=8YFLogxK
U2 - 10.1021/ac001332p
DO - 10.1021/ac001332p
M3 - Article
VL - 73
SP - 2682
EP - 2685
JO - Analytical Chemistry
JF - Analytical Chemistry
SN - 0003-2700
IS - 11
ER -