Enzymic degradation of deoxyribonucleic acid. I. Distribution of bases in fractions of calf thymus deoxyribonucleic acid hydrolysate obtained by deoxyribonuclease II

1961 ◽  
Vol 26 (11) ◽  
pp. 2739-2748 ◽  
Author(s):  
J. Doskočil ◽  
F. Šorm
1968 ◽  
Vol 108 (5) ◽  
pp. 749-753 ◽  
Author(s):  
A R Fahmy ◽  
K Griffiths

The inhibition by diethylstilboestrol of DNA nucleotidyltransferase isolated from calf thymus was studied. The inhibition exercised by diethylstilboestrol appears to obey competitive kinetics with respect to DNA primer. The activities of both replicative and terminal enzymes were affected to the same extent. There was no evidence of binding between DNA and diethylstilboestrol. A comparative study of the inhibitory effects of some stilboestrol derivatives is presented. The alkyl substitution in the αα′-positions seem to alter the inhibitory effect of these compounds: dimethylstilboestrol was more inhibitory than stilbene, and diethylstilboestrol was more inhibitory than dimethylstilboestrol. Hexoestrol, in which the αα′-ethylenic linkage is saturated, was the most effective inhibitor.


Biochemistry ◽  
1980 ◽  
Vol 19 (10) ◽  
pp. 2096-2101 ◽  
Author(s):  
Marietta Y. W. Tsang Lee ◽  
Cheng-Keat Tan ◽  
Antero G. So ◽  
Kathleen M. Downey

1958 ◽  
Vol 36 (12) ◽  
pp. 1251-1256 ◽  
Author(s):  
R. O. Hurst

The hydrolysis of deoxyribonucleic acid by pancreatic deoxyribonuclease was studied using high concentrations of enzyme. An increased production of material soluble in uranyl acetate reagent was obtained. Evidence for heterogeneity in the activity of the enzyme is presented.


2019 ◽  
Vol 43 (17) ◽  
pp. 6702-6711 ◽  
Author(s):  
Hongqin Yang ◽  
Qingle Zeng ◽  
Ze He ◽  
Di Wu ◽  
Hui Li

The binding interaction of niraparib (MK-4827), a poly(ADP-ribose) polymerase inhibitor, with calf thymus deoxyribonucleic acid (ctDNA) has been explored by various theoretical and experimental techniques.


1960 ◽  
Vol 38 (1) ◽  
pp. 347-354 ◽  
Author(s):  
R. O. Hurst ◽  
Dorothy Findlay

Hydrolysis of sodium oligonucleotide by crystalline pancreatic deoxyribonuclease (DNA-ase) has been studied in the presence of different metal ions and the chelating agent ethylenediaminetetraacetate (EDTA). Although EDTA inhibited the action of DNA-ase when magnesium or cobaltous ions were used as activator, the enzyme activity was enhanced in the presence of manganous ions and EDTA. The results are interpreted as indicating the presence of an oligonucleotidase function in the enzyme preparation. A differential assay method for DNA-ase and oligonucleotidase activity has been devised and the evidence obtained gives additional support for this conclusion.


1967 ◽  
Vol 105 (2) ◽  
pp. 673-677 ◽  
Author(s):  
J. T. O. Kirk

A method is described for determination of the base composition (as guanine+cytosine or adenine+thymine content) of DNA by accurate measurement of the adenine/guanine ratio. The DNA is hydrolysed with 0·03n-hydrochloric acid for 40min. to release the purines. The hydrolysate is subjected to ion-exchange chromatography on Zeo-Karb 225. Apurinic acids are eluted with 0·03n-hydrochloric acid and then guanine and adenine are eluted separately with 2n-hydrochloric acid. Guanine and adenine are each collected as a single fraction, and the amount of base in each case is determined by measuring the volume and the extinction at suitable wavelengths. For use in the calculations, millimolar extinction coefficients in 2n-hydrochloric acid of 12·09 for adenine at 262mμ, and 10·77 for guanine at 248mμ, were determined with authentic samples of bases. The method gives extremely reproducible results: from 12 determinations with calf thymus DNA the adenine/guanine molar ratio had a standard deviation of 0·011; this corresponds to a standard deviation in guanine+cytosine content of 0·2% guanine+cytosine.


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