Macromolecule Analysis Based on Electrophoretic Mobility in Air: Globular Proteins
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 o...
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| Veröffentlicht in: | Analytical chemistry (Washington) 1996-06, Vol.68 (11), p.1895-1904 |
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| container_issue | 11 |
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| container_title | Analytical chemistry (Washington) |
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| creator | Kaufman, Stanley L Skogen, Jeffrey W Dorman, Frank D Zarrin, Fahimeh Lewis, Kenneth C |
| description | 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. |
| doi_str_mv | 10.1021/ac951128f |
| format | Article |
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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.</description><identifier>ISSN: 0003-2700</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/ac951128f</identifier><identifier>PMID: 21619100</identifier><identifier>CODEN: ANCHAM</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Air ; Analytical biochemistry: general aspects, technics, instrumentation ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Chemistry ; Fundamental and applied biological sciences. 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Chem</addtitle><description>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.</description><subject>Air</subject><subject>Analytical biochemistry: general aspects, technics, instrumentation</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Chemistry</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Ions</topic><topic>Molecules</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kaufman, Stanley L</creatorcontrib><creatorcontrib>Skogen, Jeffrey W</creatorcontrib><creatorcontrib>Dorman, Frank D</creatorcontrib><creatorcontrib>Zarrin, Fahimeh</creatorcontrib><creatorcontrib>Lewis, Kenneth C</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Aluminium Industry Abstracts</collection><collection>Biotechnology Research Abstracts</collection><collection>Ceramic Abstracts</collection><collection>Computer and Information Systems Abstracts</collection><collection>Corrosion Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Materials Business File</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Aerospace Database</collection><collection>Copper Technical Reference Library</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical chemistry (Washington)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kaufman, Stanley L</au><au>Skogen, Jeffrey W</au><au>Dorman, Frank D</au><au>Zarrin, Fahimeh</au><au>Lewis, Kenneth C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Macromolecule Analysis Based on Electrophoretic Mobility in Air: Globular Proteins</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>1996-06-01</date><risdate>1996</risdate><volume>68</volume><issue>11</issue><spage>1895</spage><epage>1904</epage><pages>1895-1904</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><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.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>21619100</pmid><doi>10.1021/ac951128f</doi><tpages>10</tpages></addata></record> |
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| subjects | Air Analytical biochemistry: general aspects, technics, instrumentation Analytical, structural and metabolic biochemistry Biological and medical sciences Chemistry Fundamental and applied biological sciences. Psychology Ions Molecules Proteins |
| title | Macromolecule Analysis Based on Electrophoretic Mobility in Air: Globular Proteins |
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