Quantitative Footprinting Analysis. Binding to a Single Site

Robert Rehfuss; Jerry Goodisman; James C. Dabrowiak

doi:10.1021/bi00455a027

Quantitative Footprinting Analysis. Binding to a Single Site

Robert Rehfuss, Jerry Goodisman, James C. Dabrowiak

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

Abstract

The theory for measuring ligand binding constants from footprinting autoradiographic data associated with a single binding site is derived. If the ligand and DNA cleavage agent compete for a common site, the spot intensities are not proportional to the amount of DNA not blocked by ligand. The analysis of a single site is experimentally illustrated by using results for the anticancer drug actinomycin D interacting with the duplex d(TAGCGCTA)₂ as probed with the hydrolytic enzyme DNase I.

Original language	English (US)
Pages (from-to)	777-781
Number of pages	5
Journal	Biochemistry
Volume	29
Issue number	3
DOIs	https://doi.org/10.1021/bi00455a027
State	Published - Jan 1 1990

ASJC Scopus subject areas

Biochemistry

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10.1021/bi00455a027

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title = "Quantitative Footprinting Analysis. Binding to a Single Site",

abstract = "The theory for measuring ligand binding constants from footprinting autoradiographic data associated with a single binding site is derived. If the ligand and DNA cleavage agent compete for a common site, the spot intensities are not proportional to the amount of DNA not blocked by ligand. The analysis of a single site is experimentally illustrated by using results for the anticancer drug actinomycin D interacting with the duplex d(TAGCGCTA)2 as probed with the hydrolytic enzyme DNase I.",

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AB - The theory for measuring ligand binding constants from footprinting autoradiographic data associated with a single binding site is derived. If the ligand and DNA cleavage agent compete for a common site, the spot intensities are not proportional to the amount of DNA not blocked by ligand. The analysis of a single site is experimentally illustrated by using results for the anticancer drug actinomycin D interacting with the duplex d(TAGCGCTA)2 as probed with the hydrolytic enzyme DNase I.

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Quantitative Footprinting Analysis. Binding to a Single Site

Abstract

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