Purification and partial characterization of a daunorubicin-binding protein from rat liver

R. A. Gambetta; A. Colombo; C. Lanzi; F. Zunino

Purification and partial characterization of a daunorubicin-binding protein from rat liver

R. A. Gambetta, A. Colombo, C. Lanzi, F. Zunino

Fondazione IRCCS Istituto Nazionale dei Tumori

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Abstract

A daunorubicin-binding protein has been isolated from the soluble fraction of normal rat liver by affinity chromatography on daunorubicin-Sepharose columns. This protein, which apparently binds anthracyclines specifically, appears to be composed of four polypeptides of 54,000 M(r), is different from tubulin, and is not involved in anthracycline metabolism. Its physiological function remains to be determined.

Original language	English
Pages (from-to)	336-340
Number of pages	5
Journal	Molecular Pharmacology
Volume	24
Issue number	2
Publication status	Published - 1983

ASJC Scopus subject areas

Pharmacology

Cite this

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abstract = "A daunorubicin-binding protein has been isolated from the soluble fraction of normal rat liver by affinity chromatography on daunorubicin-Sepharose columns. This protein, which apparently binds anthracyclines specifically, appears to be composed of four polypeptides of 54,000 M(r), is different from tubulin, and is not involved in anthracycline metabolism. Its physiological function remains to be determined.",

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AB - A daunorubicin-binding protein has been isolated from the soluble fraction of normal rat liver by affinity chromatography on daunorubicin-Sepharose columns. This protein, which apparently binds anthracyclines specifically, appears to be composed of four polypeptides of 54,000 M(r), is different from tubulin, and is not involved in anthracycline metabolism. Its physiological function remains to be determined.

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Purification and partial characterization of a daunorubicin-binding protein from rat liver

Abstract

ASJC Scopus subject areas

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