Aerbactin Operon 의 Operator 와 Fur ( Ferric Uptake Regulation ) 단백질간의 결합하는 성질

Binding properties of Fur protein to the operator region of aerobactin operon were investigated. By nitrocellulose filter binding assay, dissociation constant of Fur-operator complex was ranged 3∼6×10^(-12) M² using Mn^(2+) as a corepressor. Hill plot of the binding isotherm indicates that the repre...

Full description

Saved in:
Bibliographic Details
Published inBMB reports Vol. 26; no. 8; pp. 726 - 732
Main Authors 위세찬, 최수영, 손정인, Se Chan Wee, Soo Young Choi, Jeong In Sohn
Format Journal Article
LanguageKorean
Published 생화학분자생물학회 01.01.1993
Online AccessGet full text

Cover

More Information
Summary:Binding properties of Fur protein to the operator region of aerobactin operon were investigated. By nitrocellulose filter binding assay, dissociation constant of Fur-operator complex was ranged 3∼6×10^(-12) M² using Mn^(2+) as a corepressor. Hill plot of the binding isotherm indicates that the repressor protein forms dimer in order to bind the operator. Stability of Fur-operator complex depends on the divalent transition metal involved in the complex. Binding affinity of the protein was not altered by the different incubation temperature. However, at higher temperature the repressor showed higher saturation level with the same amount of operator.
Bibliography:Korean Society for Biochemistry and Molecular Biology
ISSN:1976-6696