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PMID: 172646 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Properties of the Escherichia coli DNA-binding (unwinding) protein interaction with nucleolytic enzymes and DNA.

Journal of molecular biology ·Vol. 98 ·No. 4 ·1975-11-15 ·Pages 811-25

Molineux IJ, Gefter ML

Abstract

暂无摘要

MeSH Terms

Bacterial Proteins Binding Sites DNA Nucleotidyltransferases/metabolism DNA, Bacterial Deoxyribonucleases/metabolism Deoxyribonucleoproteins Escherichia coli/analysis Exonucleases/metabolism Kinetics Macromolecular Substances Nucleic Acid Conformation Phosphoric Diester Hydrolases Protein Binding

Chemicals

Bacterial Proteins DNA, Bacterial Deoxyribonucleoproteins Macromolecular Substances DNA Nucleotidyltransferases Deoxyribonucleases Exonucleases Phosphoric Diester Hydrolases

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Molineux I J

Gefter M L

Article Info

Journal

Journal of molecular biology

Abbr.

J Mol Biol

ISSN

0022-2836

DOI

10.1016/s0022-2836(75)80012-x

Published

1975-11-15

Pages

811-25

Language

English

Region

England

NLM ID

2985088R

Subset

External Links

PubMed source DOI: 10.1016/s0022-2836(75)80012-x View journal details

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Properties of the Escherichia coli DNA-binding (unwinding) protein interaction with nucleolytic enzymes and DNA.

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