Abstract
On-line capillary isoelectric focusing (CIEF)-electrospray ionization time-of-flight mass spectrometry (ESI-TOFMS) as a two-dimensional separation system is employed for high resolution analysis of model proteins (myoglobin and b-lactoglobulin) and human hemoglobin variants C, S, F, and A. The focused proteins in a polyacrylamide-coated capillary are mobilized by replacing the sodium hydroxide catholyte with a sheath liquid solution containing methanol-water-acetic acid in a volume ratio of 80:19:1. The use of sheath liquid also establishes the electrical connection at the CIEF capillary terminus, which serves to define the elearic field along the CIEF capillary and apply an electric voltage for electrospray ionization. At the end of the CIEF capillary, the mobilized protein zones are analyzed and directly identified by ESI-TOFMS. The TOFMS accumulates spectra at 5000 Hz frequency
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