HYDROLYSIS OF CALF THYMUS DEOXYRIBONUCLEATE BY PANCREATIC DEOXYRIBONUCLEASE: I. A STUDY OF THE OLIGONUCLEOTIDES LIBERATED IN THE PRESENCE OF MAGNESIUM OR MANGANESE IONS

1963 ◽  
Vol 41 (1) ◽  
pp. 469-480 ◽  
Author(s):  
R. O. Hurst ◽  
G. C. Becking
Keyword(s):  
Metal Ion ◽  
Deoxyribonucleic Acid ◽  
Exchange Chromatography ◽  
Magnesium Ions ◽  
Manganese Ions ◽  
Terminal Position ◽  
Deoxyribonuclease I ◽  
Calf Thymus ◽  
Hydrolysis Of

The oligonucleotides obtained from deoxyribonucleic acid by the action of pancreatic deoxyribonuclease in the presence of magnesium ions or manganous ions have been analyzed by ion exchange chromatography and by determination of the relative amounts of purine and pyrimidine deoxynucleotides occupying the 5′-terminal position. Evidence of a difference in the specificity of action of the enzyme that is dependent upon the nature of the metal ion activator employed has been adduced.

HYDROLYSIS OF CALF THYMUS DEOXYRIBONUCLEATE BY PANCREATIC DEOXYRIBONUCLEASE: I. A STUDY OF THE OLIGONUCLEOTIDES LIBERATED IN THE PRESENCE OF MAGNESIUM OR MANGANESE IONS

1963 ◽  
Vol 41 (2) ◽  
pp. 469-480 ◽  
Author(s):  
R. O. Hurst ◽  
G. C. Becking
Keyword(s):  
Metal Ion ◽  
Deoxyribonucleic Acid ◽  
Exchange Chromatography ◽  
Magnesium Ions ◽  
Manganese Ions ◽  
Terminal Position ◽  
Deoxyribonuclease I ◽  
Calf Thymus ◽  
Hydrolysis Of

The oligonucleotides obtained from deoxyribonucleic acid by the action of pancreatic deoxyribonuclease in the presence of magnesium ions or manganous ions have been analyzed by ion exchange chromatography and by determination of the relative amounts of purine and pyrimidine deoxynucleotides occupying the 5′-terminal position. Evidence of a difference in the specificity of action of the enzyme that is dependent upon the nature of the metal ion activator employed has been adduced.

scholarly journals Determination of the base composition of deoxyribonucleic acid by measurement of the adenine/guanine ratio

1967 ◽  
Vol 105 (2) ◽  
pp. 673-677 ◽  
Author(s):  
J. T. O. Kirk
Keyword(s):  
Standard Deviation ◽  
Hydrochloric Acid ◽  
Base Composition ◽  
Deoxyribonucleic Acid ◽  
Exchange Chromatography ◽  
Molar Ratio ◽  
Calf Thymus ◽  
Guanine And Adenine ◽  
Adenine Thymine

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.

THE DEGRADATION OF CALF THYMUS DEOXYRIBONUCLEIC ACID BY PANCREATIC DEOXYRIBONUCLEASE

1958 ◽  
Vol 36 (12) ◽  
pp. 1251-1256 ◽  
Author(s):  
R. O. Hurst
Keyword(s):  
Deoxyribonucleic Acid ◽  
Uranyl Acetate ◽  
Calf Thymus ◽  
High Concentrations ◽  
Hydrolysis Of

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.

Determination of the DNA binding properties of a novel PARP inhibitor MK-4827 with calf-thymus DNA by molecular simulations and detailed spectroscopic investigations

2019 ◽  
Vol 43 (17) ◽  
pp. 6702-6711 ◽  
Author(s):  
Hongqin Yang ◽  
Qingle Zeng ◽  
Ze He ◽  
Di Wu ◽  
Hui Li
Keyword(s):  
Dna Binding ◽  
Deoxyribonucleic Acid ◽  
Parp Inhibitor ◽  
Molecular Simulations ◽  
Binding Interaction ◽  
Binding Properties ◽  
Calf Thymus ◽  
Polymerase Inhibitor ◽  
Dna Binding Properties

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.

THE ACTION OF PANCREATIC DEOXYRIBONUCLEASE ON OLIGONUCLEOTIDES FROM CALF THYMUS DEOXYRIBONUCLEIC ACID

1960 ◽  
Vol 38 (1) ◽  
pp. 347-354 ◽  
Author(s):  
R. O. Hurst ◽  
Dorothy Findlay
Keyword(s):  
Enzyme Activity ◽  
Metal Ions ◽  
Enzyme Preparation ◽  
Deoxyribonucleic Acid ◽  
Chelating Agent ◽  
Assay Method ◽  
Calf Thymus ◽  
Additional Support ◽  
Hydrolysis Of

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.

Adsorption of Macromolecules on Mineral Fibers

1983 ◽  
Vol 2 (2) ◽  
pp. 187-192 ◽  
Author(s):  
Ming J.W. Chang ◽  
Laurie B. Joseph ◽  
Ralph E. Stephens ◽  
Ronald W. Hart
Keyword(s):  
Glass Fiber ◽  
Deoxyribonucleic Acid ◽  
Fibroblast Cell ◽  
Biological Processes ◽  
Mineral Fibers ◽  
Deoxyribonuclease I ◽  
Enzyme Substrate ◽  
Human Fibroblast Cell ◽  
Normal Human ◽  
Hydrolysis Of

Several mineral fibers were shown to adsorb differentially to three classes of biologically significant macromolecules (i.e., DNA, RNA, and protein). The cytotoxicity exerted by the particulates on a normal human fibroblast cell line, with the exception of attapulgite, correlated positively with the degree of macromolecular adsorption exhibited by these substances, namely: short chrysotile > attapulgite = intermediate chrysotile > amosite > glass fiber. Correspondingly, the ability to interfere with the enzymatic hydrolysis of deoxyribonucleic acid by bovine pancreatic deoxyribonuclease I followed a similar pattern, i.e., chrysotile > amosite = glass fiber. The results suggest that adsorption by mineral fibers may induce changes in enzyme-substrate interactions and therefore could interfere with normal biological processes.

Determination of the Interaction of Deoxyribonucleate and Magnesium Ions by Means of a Metal Ion Indicator

Nature ◽  
1959 ◽  
Vol 184 (4686) ◽  
pp. 635-636 ◽  
Author(s):  
JOSEPH SHACK ◽  
BARBARA S. BYNUM
Keyword(s):  
Metal Ion ◽  
Magnesium Ions

scholarly journals Purification and properties of the hexosaminidase A-activating protein from human liver

1977 ◽  
Vol 167 (3) ◽  
pp. 693-701 ◽  
Author(s):  
Peter Hechtman ◽  
Dorothy LeBlanc
Keyword(s):  
Human Liver ◽  
Gel Filtration ◽  
Disc Electrophoresis ◽  
Exchange Chromatography ◽  
Hydrolase Activity ◽  
Gm2 Ganglioside ◽  
Purification And Properties ◽  
Hexosaminidase A ◽  
Hydrolysis Of

Human liver extracts contain an activating protein which is required for hexosaminidase A-catalysed hydrolysis of the N-acetylgalactosaminyl linkage of GM2 ganglioside [N-acetylgalactosaminyl-(N-acetylneuraminyl) galactosylglucosylceramide]. A partially purified preparation of human liver hexosaminidase A that is substantially free of GM2 ganglioside hydrolase activity is used to assay the activating protein. The proceudres of heat and alcohol denaturation, ion-exchange chromatography and gel filtration were used to purify the activating protein over 100-fold from crude human liver extracts. When the purified activating protein is analysed by polyacrylamide-gel disc electrophoresis, two closely migrating protein bands are seen. When purified activating protein is used to reconstitute the GM2 ganglioside hydrolase activity, the rate of reaction is proportional to the amount of hexosaminidase A used. The activation is specific for GM2 ganglioside and and hexosaminidase A. The activating protein did not stimulate hydrolysis of asialo-GM2 ganglioside by either hexosaminidase A or B. Hexosaminidase B did not catalyse hydrolysis of GM2 ganglioside with or without the activator. Kinetic experiments suggest the presence of an enzyme–activator complex. The dissociation constant of this complex is decreased when higher concentrations of substrate are used, suggesting the formation of a ternary complex between enzyme, activator and substrate. Determination of the molecular weight of the activating protein by gel-filtration and sedimentation-velocity methods gave values of 36000 and 39000 respectively.

Enzymic hydrolysis of calf thymus deoxyribonucleic acid adsorbed on diethylaminoethyl cellulose

Biochemistry ◽  
1968 ◽  
Vol 7 (1) ◽  
pp. 406-411 ◽  
Author(s):  
George W. Rushizky ◽  
Isabelle H. Skavenski ◽  
Antoinette E. Greco
Keyword(s):  
Deoxyribonucleic Acid ◽  
Enzymic Hydrolysis ◽  
Calf Thymus ◽  
Diethylaminoethyl Cellulose ◽  
Hydrolysis Of
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