Organelle purification by free flow electrophoresis for comprehensive subcellular proteome analysis

U. Schneider; H. Zischka; T. Meitinger; M. Ueffing; G. Weber; P. Weber; M. Nissum; A. Posch; C. Eckerskorn

Organelle purification by free flow electrophoresis for comprehensive subcellular proteome analysis

U. Schneider, H. Zischka, T. Meitinger, M. Ueffing, G. Weber, P. Weber, M. Nissum, A. Posch, C. Eckerskorn

Medicine and Health

Publikation: Konferenzbeitrag › Papier › Begutachtung

Abstract

A raw mitochondria preparation obtained by differential centrifugation was purified by free flow electrophoresis using a Tecan Pro Team FFE instrument. The yeast strain Sc 338 (wild type yeast) was grown in rich medium and harvested by centrifugation. Fractions of different electrophoretic mobility were obtained and mitochondria were isolated by centrifugation. 2D-electrophoresis and MALDI-mass spectrometry (MS) analysis of the raw mitochondria preparation clearly demonstrated the strong presence of protein fragments and proteins of non-mitochondrial origin. The 2D-patterns of FFE purified mitochondria yielded only full length protein species of mitochondrial origin as demonstrated by more than 400 peptide mass fingerprints.

Originalsprache	Englisch
Seiten	143
Seitenumfang	1
Publikationsstatus	Veröffentlicht - 2002
Veranstaltung	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, USA/Vereinigte Staaten Dauer: 2 Juni 2002 → 6 Juni 2002

Konferenz

Konferenz	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Land/Gebiet	USA/Vereinigte Staaten
Ort	Orlando, FL
Zeitraum	2/06/02 → 6/06/02

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title = "Organelle purification by free flow electrophoresis for comprehensive subcellular proteome analysis",

abstract = "A raw mitochondria preparation obtained by differential centrifugation was purified by free flow electrophoresis using a Tecan Pro Team FFE instrument. The yeast strain Sc 338 (wild type yeast) was grown in rich medium and harvested by centrifugation. Fractions of different electrophoretic mobility were obtained and mitochondria were isolated by centrifugation. 2D-electrophoresis and MALDI-mass spectrometry (MS) analysis of the raw mitochondria preparation clearly demonstrated the strong presence of protein fragments and proteins of non-mitochondrial origin. The 2D-patterns of FFE purified mitochondria yielded only full length protein species of mitochondrial origin as demonstrated by more than 400 peptide mass fingerprints.",

author = "U. Schneider and H. Zischka and T. Meitinger and M. Ueffing and G. Weber and P. Weber and M. Nissum and A. Posch and C. Eckerskorn",

year = "2002",

language = "English",

pages = "143",

note = "Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics ; Conference date: 02-06-2002 Through 06-06-2002",

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TY - CONF

T1 - Organelle purification by free flow electrophoresis for comprehensive subcellular proteome analysis

AU - Schneider, U.

AU - Zischka, H.

AU - Meitinger, T.

AU - Ueffing, M.

AU - Weber, G.

AU - Weber, P.

AU - Nissum, M.

AU - Posch, A.

AU - Eckerskorn, C.

PY - 2002

Y1 - 2002

N2 - A raw mitochondria preparation obtained by differential centrifugation was purified by free flow electrophoresis using a Tecan Pro Team FFE instrument. The yeast strain Sc 338 (wild type yeast) was grown in rich medium and harvested by centrifugation. Fractions of different electrophoretic mobility were obtained and mitochondria were isolated by centrifugation. 2D-electrophoresis and MALDI-mass spectrometry (MS) analysis of the raw mitochondria preparation clearly demonstrated the strong presence of protein fragments and proteins of non-mitochondrial origin. The 2D-patterns of FFE purified mitochondria yielded only full length protein species of mitochondrial origin as demonstrated by more than 400 peptide mass fingerprints.

AB - A raw mitochondria preparation obtained by differential centrifugation was purified by free flow electrophoresis using a Tecan Pro Team FFE instrument. The yeast strain Sc 338 (wild type yeast) was grown in rich medium and harvested by centrifugation. Fractions of different electrophoretic mobility were obtained and mitochondria were isolated by centrifugation. 2D-electrophoresis and MALDI-mass spectrometry (MS) analysis of the raw mitochondria preparation clearly demonstrated the strong presence of protein fragments and proteins of non-mitochondrial origin. The 2D-patterns of FFE purified mitochondria yielded only full length protein species of mitochondrial origin as demonstrated by more than 400 peptide mass fingerprints.

UR - http://www.scopus.com/inward/record.url?scp=2442705607&partnerID=8YFLogxK

M3 - Paper

AN - SCOPUS:2442705607

SP - 143

T2 - Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics

Y2 - 2 June 2002 through 6 June 2002

ER -

Organelle purification by free flow electrophoresis for comprehensive subcellular proteome analysis

Abstract

Konferenz

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