Use of anion-exchange chromatography and chromatofocusing to reveal the structural and functional heterogeneity of topoisomerase II in a HL-60 cell line resistant to multi-drug treatment

Fritz Boege; Frank Gieseler; Harald Biersack; Michael Clark

doi:10.1016/0021-9673(91)85191-H

Use of anion-exchange chromatography and chromatofocusing to reveal the structural and functional heterogeneity of topoisomerase II in a HL-60 cell line resistant to multi-drug treatment

Fritz Boege^*, Frank Gieseler, Harald Biersack, Michael Clark

^*Korrespondierende/r Autor/-in für diese Arbeit

Medizinische Klinik I

Julius-Maximilians-Universität Würzburg

5 Zitate (Scopus)

Abstract

Fractionation of nuclear extracts from a multi-drug-resistant subclone of the human promyelocytic subline HL-60 by anion-exchange chromatography and chromatofocusing resolves at least two different subtypes of topoisomerase II, which are not identical to the known α- and β-forms of the enzyme because both forms are contained in each subtype. The two subtypes are present in about equal proportions and differ remarkably with respect to the optimum of reaction and sensitivity to m-amsacrine and orthovanadate. Both subtypes are highly insensitive to etoposide inhibition in vitro.

Originalsprache	Englisch
Zeitschrift	Journal of Chromatography A
Jahrgang	587
Ausgabenummer	1
Seiten (von - bis)	3-9
Seitenumfang	7
ISSN	0021-9673
DOIs	https://doi.org/10.1016/0021-9673(91)85191-H
Publikationsstatus	Veröffentlicht - 29.11.1991

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10.1016/0021-9673(91)85191-H

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@article{6060c1e683e94fa88447d6fa6dcc9bf1,

title = "Use of anion-exchange chromatography and chromatofocusing to reveal the structural and functional heterogeneity of topoisomerase II in a HL-60 cell line resistant to multi-drug treatment",

abstract = "Fractionation of nuclear extracts from a multi-drug-resistant subclone of the human promyelocytic subline HL-60 by anion-exchange chromatography and chromatofocusing resolves at least two different subtypes of topoisomerase II, which are not identical to the known α- and β-forms of the enzyme because both forms are contained in each subtype. The two subtypes are present in about equal proportions and differ remarkably with respect to the optimum of reaction and sensitivity to m-amsacrine and orthovanadate. Both subtypes are highly insensitive to etoposide inhibition in vitro.",

author = "Fritz Boege and Frank Gieseler and Harald Biersack and Michael Clark",

note = "Funding Information: This work was supported in part by the Wilhelm-Sander Stiftung, Grant 90 .038 .1, to F .B . and the Deutsche Forschungsgemeinschaft, SFB 172 .. C9 . (F .G .) . The authors are indebted to Professor L . F . Liu for the gift of the rabbit anti-human topoisom-erase II antiserum .",

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doi = "10.1016/0021-9673(91)85191-H",

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Use of anion-exchange chromatography and chromatofocusing to reveal the structural and functional heterogeneity of topoisomerase II in a HL-60 cell line resistant to multi-drug treatment. / Boege, Fritz; Gieseler, Frank ; Biersack, Harald et al.
in: Journal of Chromatography A, Jahrgang 587, Nr. 1, 29.11.1991, S. 3-9.

Publikation: Beiträge in Fachzeitschriften › Zeitschriftenaufsätze › Forschung › Begutachtung

TY - JOUR

T1 - Use of anion-exchange chromatography and chromatofocusing to reveal the structural and functional heterogeneity of topoisomerase II in a HL-60 cell line resistant to multi-drug treatment

AU - Boege, Fritz

AU - Gieseler, Frank

AU - Biersack, Harald

AU - Clark, Michael

N1 - Funding Information: This work was supported in part by the Wilhelm-Sander Stiftung, Grant 90 .038 .1, to F .B . and the Deutsche Forschungsgemeinschaft, SFB 172 .. C9 . (F .G .) . The authors are indebted to Professor L . F . Liu for the gift of the rabbit anti-human topoisom-erase II antiserum .

PY - 1991/11/29

Y1 - 1991/11/29

N2 - Fractionation of nuclear extracts from a multi-drug-resistant subclone of the human promyelocytic subline HL-60 by anion-exchange chromatography and chromatofocusing resolves at least two different subtypes of topoisomerase II, which are not identical to the known α- and β-forms of the enzyme because both forms are contained in each subtype. The two subtypes are present in about equal proportions and differ remarkably with respect to the optimum of reaction and sensitivity to m-amsacrine and orthovanadate. Both subtypes are highly insensitive to etoposide inhibition in vitro.

AB - Fractionation of nuclear extracts from a multi-drug-resistant subclone of the human promyelocytic subline HL-60 by anion-exchange chromatography and chromatofocusing resolves at least two different subtypes of topoisomerase II, which are not identical to the known α- and β-forms of the enzyme because both forms are contained in each subtype. The two subtypes are present in about equal proportions and differ remarkably with respect to the optimum of reaction and sensitivity to m-amsacrine and orthovanadate. Both subtypes are highly insensitive to etoposide inhibition in vitro.

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