Sheathless capillary electrophoresis-electrospray ionization mass spectrometry using 10 μm I.D. capillaries: Analyses of tryptic digests of cytochrome c
| Autor: | Jon H. Wahl, David C. Gale, Richard D. Smith |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Electrophoresis
Electrospray Capillary action Electrospray ionization Molecular Sequence Data Analytical chemistry Cytochrome c Group Mass spectrometry Biochemistry Mass Spectrometry Analytical Chemistry Capillary electrophoresis Ionization Animals Trypsin Amino Acid Sequence Horses Candida Gel electrophoresis Chromatography biology Chemistry Cytochrome c Organic Chemistry General Medicine Peptide Fragments Evaluation Studies as Topic biology.protein Cattle |
| Zdroj: | Journal of Chromatography A. 659:217-222 |
| ISSN: | 0021-9673 |
| Popis: | The analyses of tryptic digest of proteins present a difficult challenge to the analytical chemist due to the wide range of molecular masses and hydrophobicities of the peptides produced. In this study, we demonstrate the separation of tryptic digests of bovine, Candida krusei and equine cytochrome c using a new electrospray ionization (ESI) interface for CE-MS that does not require additional sheath make-up fluid or mechanical assistance to aid the ESI process. The utility of this new CE-ESI-MS interface is demonstrated using a 10 microm I.D. CE capillary where the injected sample amounts are in the 30 femtomole (of protein) region. The CE electroosmotic flow rates when aminopropylamine treated capillaries are utilized are in the 10 nl/min region for a relatively conductive buffer system (0.01 M ammonium acetate-acetic acid buffer system, pH 4.4 and a 300 V/cm field strength). |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|