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Macromolecule Analysis Based on Electrophoretic Mobility in Air: Globular Proteins

Kaufman, Stanley L., Skogen, Jeffrey W., Dorman, Frank D., Zarrin, Fahimeh, Lewis, Kenneth C.·1996·Analytical Chemistry

Abstract

Globular proteins ranging in molecular mass from 5.7 to 669 kDa were separated and analyzed using an aerosol technique based on the electrophoretic mobility of singly-charged molecular ions in air. The ions were produced by electrospraying and drying 100-nm-diameter droplets of a liquid suspension of the proteins, using ionized air to remove the droplet charge due to the spray process. The electrophoretic mobility was measured using a modified commercial continuous-flow differential mobility analyzer operated near atmospheric pressure. An unmodified commercial condensation particle counter was used for detection. The concentrations analyzed ranged from 0.02 to 200 μg of protein/mL of buffer, with a liquid sample flow rate of approximately 50 nL/min. Sampling time of 3 min was used for each complete distribution measured. The electrophoretic mobilities measured were determined entirely from air flow rates, apparatus geometry, and applied potentials. Results were expressed as electrophoretic mobility equivalent diameters using a Millikan formula.

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Metadata

Authors
Kaufman, S. L., Skogen, J. W., Dorman, F. D., Zarrin, F., & Lewis, K. C.
Venue
Analytical Chemistry
Published
1996-06-01
Volume
68
Issue
11
Pages
1895-1904
ISSN
  • 0003-2700 (ISSN-L)
  • 1520-6882
OpenAlex
W1966985858
Cited by
218
References
0
FWCI
4.60
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Macromolecule Analysis Based on Electrophoretic Mobility in Air: Globular Proteins. https://app.cochat.ai/papers/10.1021/ac951128f
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Kaufman, S. L., Skogen, J. W., Dorman, F. D., Zarrin, F., & Lewis, K. C. (1996). Macromolecule Analysis Based on Electrophoretic Mobility in Air: Globular Proteins. Analytical Chemistry. https://doi.org/10.1021/ac951128f

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