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.

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

1960 ◽  
Vol 38 (4) ◽  
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.

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.

THE HETEROGENEITY OF PANCREATIC DEOXYRIBONUCLEASE

1962 ◽  
Vol 40 (2) ◽  
pp. 165-175 ◽  
Author(s):  
G. C. Becking ◽  
R. O. Hurst
Keyword(s):  
Enzyme Activity ◽  
Ionic Strength ◽  
Enzyme Preparation ◽  
Deoxyribonucleic Acid ◽  
Paper Electrophoresis ◽  
Relative Activity ◽  
Enzyme Concentration ◽  
Uranyl Acetate ◽  
Ph Optimum

The action of crystalline pancreatic deoxyribonuclease on sodium oligonucleotides in the presence of manganous ions has been studied and a pH optimum of 6.6 observed. Inhibition of the enzyme activity by increased ionic strength of the digest occurred. The liberation of products soluble in uranyl acetate – trichloroacetate was found to vary with enzyme concentration and the relative activity of the enzyme on oligonucleotides was best determined by a logarithm-plot method. The activity of the enzyme towards deoxyribonucleic acid or sodium oligonucleotides as substrate was not affected by treatment with acetone. Evidence of heterogeneity in the crystalline enzyme preparation was obtained using paper electrophoresis and chromatography on carboxymethylcellulose. Two fractions were separated that showed different ratios of activity towards the two substrates employed.

scholarly journals Peptidolytic enzymes in different larval stadium of housefly Musca domestica

2012 ◽  
Vol 51 (No. 4) ◽  
pp. 139-144 ◽  
Author(s):  
J. Blahovec ◽  
Z. Kostecka ◽  
A. Kocisova
Keyword(s):  
Enzyme Activity ◽  
Metal Ions ◽  
Larval Development ◽  
Musca Domestica ◽  
Major Part ◽  
Chelating Agent ◽  
Chromogenic Substrates ◽  
Three Stages ◽  
Specific Inhibitors

Four classes of peptidolytic enzymes were described in insects. Many authors have found predominant activity belonging to trypsin-like and chymotrypsin-like activity. By the use specific chromogenic substrates and hemoglobin we have determined enzyme activity in three stages of larval development of housefly. In contrast to above mentioned data we have found, that major part of peptidolytic activity in this insect is of aminopeptidase nature. Other observed peptidolytic activity formed only minority part. Apparently the highest activities to all examined substrates were found in first larval stadium of housefly. Inhibitory studies by class specific inhibitors and influence of metal ions and chelating agent on enzyme activity have shown, that aminopeptidase-like enzymes belong to metalloproteinase group.

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

scholarly journals Effects of Some Alkali and Alkaline Earth Metal Ions on the Initial Reaction Rates of Congregibacter litoralis KT71 β-lactamase Hydrolysis of 4-Nitrophenyl Myristate

2021 ◽  
pp. 23-29
Author(s):  
O. M. Iniaghe ◽  
O. Ibukun
Keyword(s):  
Enzyme Activity ◽  
Metal Ions ◽  
Alkaline Earth ◽  
Earth Metal ◽  
Reaction Rates ◽  
Alkaline Earth Metal ◽  
Alkali Metal Ions ◽  
Initial Reaction ◽  
Alkaline Earth Metal Ions ◽  
Hydrolysis Of

The effects of some alkali metal ions (Na+ and K+) and alkaline earth metal ions (Mg 2+ and Ba2+) on the initial reaction rates of Congregibacter litoralis KT71 β-lactamase hydrolysis of 4-nitrophenyl myristate was investigated by varying the concentrations of the metal ions in the assay mixture which comprised of 100 µl of standard enzyme solution, 200 µl of varying concentration of metal ions, 500 µl of 50 mM sodium phosphate buffer pH 7.5 and 200 µl of 4-nitrophenyl myristate (substrate) which was added last to the assay mixture after an incubation time of 10 minutes at 44 oC. The enzyme activity was measured spectrophotometrically using a UV-780 recording spectrophotometer at a wavelength of 405 nm. The hydrolysis of 4-nitrophenyl myristate to yield 4-nitrophenol was monitored by reading the absorbance at 25 minutes. Results showed that the alkaline earth metal ions (Ba2+ and Mg2+) had higher enzyme activation effect than the alkali metal ions (K+ and Na+) Also, all metal ions except Mg2+ showed enzyme stimulatory effect at low concentrations (<2 mM) but inhibitory at higher ion concentrations (2 mM - 3 mM). Mg 2+ caused a proportionate decrease in enzyme activity from its peak (when metal ion concentration was lowest). Results from this research is of great significance to the industrialist especially where the search for novel lipases with unique characteristics suitable for the industries are inevitable.

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.

THE DEGRADATION OF CALF THYMUS DEOXYRIBONUCLEIC ACID BY PANCREATIC DEOXYRIBONUCLEASE

1958 ◽  
Vol 36 (1) ◽  
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.

THE HETEROGENEITY OF PANCREATIC DEOXYRIBONUCLEASE

1962 ◽  
Vol 40 (1) ◽  
pp. 165-175 ◽  
Author(s):  
G. C. Becking ◽  
R. O. Hurst
Keyword(s):  
Enzyme Activity ◽  
Ionic Strength ◽  
Enzyme Preparation ◽  
Deoxyribonucleic Acid ◽  
Paper Electrophoresis ◽  
Relative Activity ◽  
Enzyme Concentration ◽  
Uranyl Acetate ◽  
Ph Optimum

The action of crystalline pancreatic deoxyribonuclease on sodium oligonucleotides in the presence of manganous ions has been studied and a pH optimum of 6.6 observed. Inhibition of the enzyme activity by increased ionic strength of the digest occurred. The liberation of products soluble in uranyl acetate – trichloroacetate was found to vary with enzyme concentration and the relative activity of the enzyme on oligonucleotides was best determined by a logarithm-plot method. The activity of the enzyme towards deoxyribonucleic acid or sodium oligonucleotides as substrate was not affected by treatment with acetone. Evidence of heterogeneity in the crystalline enzyme preparation was obtained using paper electrophoresis and chromatography on carboxymethylcellulose. Two fractions were separated that showed different ratios of activity towards the two substrates employed.

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