DOI: 10.1111/j.1432-1033.1973.tb03044.x. Poly(Adenosine Diphosphoribose) Polymerase in Mammalian Nuclei

Poly(Adenosine Diphosphoribose) Polymerase in Mammalian Nuclei

10.1111/j.1432-1033.1973.tb03044.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

1. The ability of isolated LS‐cell nuclei to incorporate [adenine‐3H]‐NAD into acid‐insoluble products is demonstrated.2. The incorporation has a pH optimum at 8.5 and an apparent temperature optimum at 25 °C.3. The optimum Mg2+ concentration is dependent upon the NAD concentration; at 1.5 μM NAD it is 2 mM; at 1.5 mM NAD it is 3 mM; and at 9 mM NAD it is above 20 mM Mg2+ Mg2+ can be replaced by Ca2+.4. Dithiothreitol or mercaptoethanol, up to 10 mM, enhances the incorporation of NAD.5. With the optimal conditions the incorporation of NAD (V) is 128 nmol NAD×5 min−1×mg DNA−1 and the Km is 1.47 ± 0.18 mM. Nicotinamide inhibits the incorporation competitively with a Ki of 14.3 ± 1 μM and thymidine inhibits competitively with a Ki of 32.5 μM.6. The incorporation is not affected by added DNA or poly(U). It is not affected by ribonuclease but is inhibited by about 50% on treatment with deoxyribonuclease.7. The enzyme system is unstable and the decay is temperature‐dependent; there is little decay at 0 °C but above this temperature the rate of decay follows an Arrhenius relationship. The initial rates of enzyme activity also show a temperature dependence with a linear Arrhenius plot. The temperature optimum at 25 °C is the arithmetic result of these two opposing processes.

Bibliography

Stone, P. R., & Shall, S. (1973). Poly(Adenosine Diphosphoribose) Polymerase in Mammalian Nuclei. European Journal of Biochemistry, 38(1), 146â152. Portico.

Authors 2

Peter R. Stone (first)
Sydney Shall (additional)

References 38 Referenced 19

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{'key': 'e_1_2_3_12_2', 'first-page': '145', 'volume': '65', 'author': 'Otake H.', 'year': '1969', 'journal-title': 'J. Biochem. (Tokyo)'} / J. Biochem. (Tokyo) by Otake H. (1969)
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{'key': 'e_1_2_3_18_2', 'first-page': '848', 'volume': '353', 'author': 'Hilz H.', 'year': '1972', 'journal-title': "Hoppe-Seyler's Z. Physiol. Chem."} / Hoppe-Seyler's Z. Physiol. Chem. by Hilz H. (1972)
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Dates

Type	When
Created	20 years, 5 months ago (March 4, 2005, 6:43 a.m.)
Deposited	1 year, 9 months ago (Nov. 23, 2023, 10:55 a.m.)
Indexed	1 year, 9 months ago (Nov. 23, 2023, 11:10 a.m.)
Issued	52 years ago (Sept. 1, 1973)
Published	52 years ago (Sept. 1, 1973)
Published Online	20 years, 5 months ago (March 3, 2005)
Published Print	52 years ago (Sept. 1, 1973)

Funders 0

None

BibTeX

@article{Stone_1973, title={Poly(Adenosine Diphosphoribose) Polymerase in Mammalian Nuclei: Characterization of the Activity in Mouse Fibroblasts (LS Cells)}, volume={38}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1973.tb03044.x}, DOI={10.1111/j.1432-1033.1973.tb03044.x}, number={1}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={Stone, Peter R. and Shall, Sydney}, year={1973}, month=sep, pages={146–152} }

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  "abstract": "<jats:p>1. The ability of isolated LS\u2010cell nuclei to incorporate [<jats:italic>adenine</jats:italic>\u2010<jats:sup>3</jats:sup>H]\u2010NAD into acid\u2010insoluble products is demonstrated.</jats:p><jats:p>2. The incorporation has a pH optimum at 8.5 and an apparent temperature optimum at 25 \u00b0C.</jats:p><jats:p>3. The optimum Mg<jats:sup>2+</jats:sup> concentration is dependent upon the NAD concentration; at 1.5 \u03bcM NAD it is 2 mM; at 1.5 mM NAD it is 3 mM; and at 9 mM NAD it is above 20 mM Mg<jats:sup>2+</jats:sup> Mg<jats:sup>2+</jats:sup> can be replaced by Ca<jats:sup>2+</jats:sup>.</jats:p><jats:p>4. Dithiothreitol or mercaptoethanol, up to 10 mM, enhances the incorporation of NAD.</jats:p><jats:p>5. With the optimal conditions the incorporation of NAD (<jats:italic>V</jats:italic>) is 128 nmol NAD\u00d75 min<jats:sup>\u22121</jats:sup>\u00d7mg DNA<jats:sup>\u22121</jats:sup> and the <jats:italic>K</jats:italic><jats:sub>m</jats:sub> is 1.47 \u00b1 0.18 mM. Nicotinamide inhibits the incorporation competitively with a <jats:italic>K</jats:italic><jats:sub>i</jats:sub> of 14.3 \u00b1 1 \u03bcM and thymidine inhibits competitively with a <jats:italic>K</jats:italic><jats:sub>i</jats:sub> of 32.5 \u03bcM.</jats:p><jats:p>6. The incorporation is not affected by added DNA or poly(U). It is not affected by ribonuclease but is inhibited by about 50% on treatment with deoxyribonuclease.</jats:p><jats:p>7. The enzyme system is unstable and the decay is temperature\u2010dependent; there is little decay at 0 \u00b0C but above this temperature the rate of decay follows an Arrhenius relationship. The initial rates of enzyme activity also show a temperature dependence with a linear Arrhenius plot. The temperature optimum at 25 \u00b0C is the arithmetic result of these two opposing processes.</jats:p>",
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