Capillary zone electrophoresis–mass spectrometry with electrospray ionization of peptides and proteins
✍ Scribed by Joseph A. Loo; Harlan K. Jones; Harold R. Udseth; Richard D. Smith
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 504 KB
- Volume
- 1
- Category
- Article
- ISSN
- 1040-7685
No coin nor oath required. For personal study only.
✦ Synopsis
Capillary zone electrophoresis (CZE) coupled with an on-line mass spectrometric (MS) detection system by an atmospheric pressure electrospray ionization (ESI) interface has been used successfully for separations of peptide and protein mixtures. For CZE-MS, ESI produces multiply charged molecular ions and thus allows m a s spectrometers with a limited mass-to-charge range to analyze proteins having molecular weights greater than 100,000. Various pH buffer systems have been investigated, including buffer systems in which pH > p1 (isoelectric point of analytes) and pH << pl are designed to reduce protein adsorption onto silica capillary surfaces and thus improve separation efficiencies. More than 125,000 theoretical plates have been obtained from a CZE-MS separation of less than 1 pmol per component of leucine enkephalin and horse heart myoglobin. CZE-MS of other large peptides and proteins are demonstrated.
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A series of newly synthesized peptides (M,= 1600-2250 Da), corresponding to portions of the extracellular domain of human granulocyte-macrophage colony stimulating factor receptor a subunit have been examined by capillary zone electrophoresis/electrospray-mass spectrometry (CZE/ES-MS). The separatio
On-line capillary zone electrophoresis/electrospray ionization mass spectrometry (CZE-ESMS) and capillary isoelectric focusing/electrospray ionization mass spectrometry (CIEF/ESMS) were employed for protein analysis. The separation mechanisms and the detection limits of CZE/ESMS and CIEF/ESMS were c