Cleavage of deoxyribonucleic acid by the 1,10-phenanthroline-cuprous complex. Hydrogen peroxide requirement and primary and secondary structure specificity

Biochemistry ◽  
1981 ◽  
Vol 20 (2) ◽  
pp. 244-250 ◽  
Author(s):  
Laura E. Marshall ◽  
Daniel R. Graham ◽  
Karl A. Reich ◽  
David S. Sigman
1971 ◽  
Vol 19 (12) ◽  
pp. 761-765 ◽  
Author(s):  
MANUEL DIAZ ◽  
JOSE HIERRO ◽  
GRACIELA DEMICHELI DE DIAZ

A new method is proposed to study the secondary structure of deoxyribonucleic acid (DNA) in situ in fixed chromatin. It is based on acriflavine staining and on differentiation with a nitrous acid solution of the fixed cytologic preparation. The presence of green fluorescence after this treatment is regarded as indicative of double stranded DNA. Experiments are described with DNA-acriflavine mixtures in solution, DNA-agar models and cytologic preparations submitted to different pretreatments. The feasibility and limitations of the method are discussed in the light of the results reported upon.


1990 ◽  
Vol 121 (3) ◽  
pp. 338 ◽  
Author(s):  
William F. Blakely ◽  
Alfred F. Fuciarelli ◽  
Brent J. Wegher ◽  
Miral Dizdaroglu

Nanoscale ◽  
2018 ◽  
Vol 10 (12) ◽  
pp. 5503-5514 ◽  
Author(s):  
Guiyang Zhang ◽  
Qiaobo Liao ◽  
Yanfeng Liu ◽  
Li Wang ◽  
Huilin Gou ◽  
...  

The secondary structure-induced aggregations pave new avenues for developing novel self-assembled nanoarchitectures with multifunctional applications.


1998 ◽  
Vol 53 (5-6) ◽  
pp. 378-382 ◽  
Author(s):  
Yoshihiro Ishikawa ◽  
Sayo Ito ◽  
Satsohi Nishino ◽  
Shigeru Ohba ◽  
Yuzo Nishida

Abstract Copper(II)-peroxide Adduct, Modification of Protein, Copper(II)-peptide Complex We have found that copper(II) compounds containing a peptide group in the chelate exhibit high activity for modification or degradation of albumin in the presence of hydrogen peroxide, whereas no activity was detected for the copper(II) compounds without an amide-group. It is suggested that presence of the amide-group in the ligand may play an important role in the formation of a peroxide adduct and in activation of the peroxide ion, leading to cleavage of the peptide bond of a neighboring protein. It is implied that conversion of normal cellular prion protein PrPC into a disease-causing isoform, PrPSc is attributed to the activated peroxide ion coordinated to a copper(II) captured in the NH2-terminal domain of the PrPC .


1976 ◽  
Vol 159 (3) ◽  
pp. 615-620 ◽  
Author(s):  
A M Campbell

The secondary structure of supercoiled DNA was varied by changes in ionic strength. For I = 0.075-0.4 the structure remained in the previously established branched form with only minor alterations in molecular dimensions. In 4M-NaCl, which induces linear DNA to change its secondary structure to the C structure and brings about an increase in the superhelix density of the molecule, no extra branches were observed on the molecules. The limiting factors that dictate supercoil structure seem to be the number and position of potential branch points and the proximity with which the two intertwining DNA strands can approach each other on the arms of the branches. This value is close to 10nm under the conditions described, and is 14-15nm at I = 0.2. It is suggested that such values should be borne in mind when models of chromosome structure are being constructed.


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