Structure of deoxyribonucleoproteins. III. Spectroscopic characterization of the ethidium bromide binding sites

Lynne M. Angerer; S. Georghiou; E. N. Moudrianakis

doi:10.1021/bi00703a003

Structure of deoxyribonucleoproteins. III. Spectroscopic characterization of the ethidium bromide binding sites

Biochemistry ◽

10.1021/bi00703a003 ◽

1974 ◽

Vol 13 (6) ◽

pp. 1075-1082 ◽

Cited By ~ 42

Author(s):

Lynne M. Angerer ◽

S. Georghiou ◽

E. N. Moudrianakis

Keyword(s):

Ethidium Bromide ◽

Binding Sites ◽

Spectroscopic Characterization

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Multiple U2AF65 Binding Sites within SF3b155: Thermodynamic and Spectroscopic Characterization of Protein–Protein Interactions among pre-mRNA Splicing Factors

Journal of Molecular Biology ◽

10.1016/j.jmb.2005.11.067 ◽

2006 ◽

Vol 356 (3) ◽

pp. 664-683 ◽

Cited By ~ 49

Author(s):

Karen R. Thickman ◽

Matthew C. Swenson ◽

Joseph M. Kabogo ◽

Zygmunt Gryczynski ◽

Clara L. Kielkopf

Keyword(s):

Protein Interactions ◽

Binding Sites ◽

Spectroscopic Characterization ◽

Mrna Splicing ◽

Splicing Factors ◽

Protein Protein Interactions

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FTIR spectroscopic characterization of the QAand QB binding sites in Rhodobacter sphaeroides R26 reaction centres

The Reaction Center of Photosynthetic Bacteria ◽

10.1007/978-3-642-61157-5_31 ◽

1996 ◽

pp. 395-404 ◽

Cited By ~ 1

Author(s):

R. Brudler ◽

H.J.M. de Groot ◽

W.B.S. van Liemt ◽

P. Gast ◽

A.J. Hoff ◽

...

Keyword(s):

Rhodobacter Sphaeroides ◽

Binding Sites ◽

Spectroscopic Characterization ◽

Reaction Centres

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Rapid Fluorescence Spectroscopic Characterization of Salivary DNA of Normal Subjects and OSCC Patients Using Ethidium Bromide

Journal of Fluorescence ◽

10.1007/s10895-014-1482-0 ◽

2015 ◽

Vol 25 (1) ◽

pp. 79-85 ◽

Cited By ~ 4

Author(s):

Manoharan Yuvaraj ◽

Prakasarao Aruna ◽

Dornadula Koteeswaran ◽

Palraj Tamilkumar ◽

Singaravelu Ganesan

Keyword(s):

Ethidium Bromide ◽

Normal Subjects ◽

Spectroscopic Characterization

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Spectroscopic Characterization of the Heme-Binding Sites inPlasmodium falciparumHistidine-Rich Protein 2†

Biochemistry ◽

10.1021/bi991665k ◽

1999 ◽

Vol 38 (51) ◽

pp. 16916-16924 ◽

Cited By ~ 45

Author(s):

Clara Y. H. Choi ◽

Jose F. Cerda ◽

Hsiu-An Chu ◽

Gerald T. Babcock ◽

Michael A. Marletta

Keyword(s):

Binding Sites ◽

Spectroscopic Characterization ◽

Heme Binding

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Spectroscopic Characterization of the Metal-Binding Sites in the Periplasmic Metal-Sensor Domain of CnrX fromCupriavidus metalliduransCH34

Biochemistry ◽

10.1021/bi201031q ◽

2011 ◽

Vol 50 (42) ◽

pp. 9036-9045 ◽

Cited By ~ 8

Author(s):

Juliette Trepreau ◽

Eve de Rosny ◽

Carole Duboc ◽

Géraldine Sarret ◽

Isabelle Petit-Hartlein ◽

...

Keyword(s):

Metal Binding ◽

Binding Sites ◽

Spectroscopic Characterization ◽

Metal Binding Sites ◽

Metal Sensor

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Characterization of Thromboxane A2/Prostaglandin H2 Receptors in Porcine Coronary Artery -The Inhibitory Effect of a Novel Dibenzoxepin Derivative, KW-3635

Thrombosis and Haemostasis ◽

10.1055/s-0038-1648498 ◽

1992 ◽

Vol 67 (05) ◽

pp. 582-584 ◽

Cited By ~ 2

Author(s):

Ichiro Miki ◽

Akio Ishii

Keyword(s):

Coronary Artery ◽

Binding Sites ◽

Thromboxane A2 ◽

Inhibitory Effect ◽

Scatchard Analysis ◽

Single Class ◽

Porcine Coronary Artery ◽

Equilibrium Binding ◽

H2 Receptors

SummaryWe characterized the thromboxane A2/prostaglandin H2 receptors in porcine coronary artery. The binding of [3H]SQ 29,548, a thromboxane A2 antagonist, to coronary arterial membranes was saturable and displaceable. Scatchard analysis of equilibrium binding showed a single class of high affinity binding sites with a dissociation constant of 18.5 ±1.0 nM and the maximum binding of 80.7 ± 5.2 fmol/mg protein. [3H]SQ 29,548 binding was concentration-dependently inhibited by thromboxane A2 antagonists such as SQ 29,548, BM13505 and BM13177 or the thromboxane A2 agonists such as U46619 and U44069. KW-3635, a novel dibenzoxepin derivative, concentration-dependently inhibited the [3H]SQ 29,548 binding to thromboxane A2/prosta-glandin H2 receptors in coronary artery with an inhibition constant of 6.0 ± 0.69 nM (mean ± S.E.M.).

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