Purification and further characterization of three DNA polymerases of rat ascites hepatoma cells
Three DNA polymerases have been isolated from rat ascites hepatoma cells and the properties of the reactions have been investigated. A polymerase (cytoplasmic polymerase: polymerase C) has been purified 560-fold from the soluble fraction of the cells and two different DNA polymerases (polymerase P-1...
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| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1974 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: BBA Section Nucleic Acids And Protein Synthesis - Amsterdam : Elsevier, 353(1974), 2, Seite 146-159 |
| Übergeordnetes Werk: |
volume:353 ; year:1974 ; number:2 ; pages:146-159 |
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| 520 | |a Three DNA polymerases have been isolated from rat ascites hepatoma cells and the properties of the reactions have been investigated. A polymerase (cytoplasmic polymerase: polymerase C) has been purified 560-fold from the soluble fraction of the cells and two different DNA polymerases (polymerase P-1 and P-2) have been purified about 70- and 60-fold, respectively, from the nuclear membrane chromatin fraction of the cells. Polymerase C has a low level of exonuclease activity but both preparations of P-1 and P-2 have no detectable nuclease activity.ATP stimulates DNA synthesis by nuclei and nuclear membrane chromatin fraction but has no stimulating effect on the purified polymerases. The activities of polymerase C and P-1 are strongly inhibited by 0.8 mM p-chloromercuribenzoate and by 1 mM N-ethylmaleimide, while only 17% and 23% inhibitions are observed with P-2, respectively. Ethanol inhibits the reaction with polymerase C and P-1, but stimulates P-2 reaction. The pH optimum of polymerase C is 7.0 in potassium phosphate buffer and that of P-1 is 6.3 in potassium phosphate, 7.3 in Tris-HCl, and 8.5 in glycine-KOH buffer. The pH optimum of P-2 is 9.8 in glycine-KOH buffer. Native DNA is more effective than heat-denatured DNA as a template for three polymerases, but activated DNA is far more effective than native DNA. Digestion of activated DNA with exonuclease III results in increases of template activity for polymerase C and P-1, but the increase with P-1 is very small. While for P-2 polymerase, no stimulating effect was observed. Poly[d(A-T) . poly[d(T-A)] is more effective than activated DNA for P-2 enzyme. | ||
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(DE-627)NLEJ185894097 (DE-599)GBVNLZ185894097 DE-627 ger DE-627 rakwb eng Purification and further characterization of three DNA polymerases of rat ascites hepatoma cells 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Three DNA polymerases have been isolated from rat ascites hepatoma cells and the properties of the reactions have been investigated. A polymerase (cytoplasmic polymerase: polymerase C) has been purified 560-fold from the soluble fraction of the cells and two different DNA polymerases (polymerase P-1 and P-2) have been purified about 70- and 60-fold, respectively, from the nuclear membrane chromatin fraction of the cells. Polymerase C has a low level of exonuclease activity but both preparations of P-1 and P-2 have no detectable nuclease activity.ATP stimulates DNA synthesis by nuclei and nuclear membrane chromatin fraction but has no stimulating effect on the purified polymerases. The activities of polymerase C and P-1 are strongly inhibited by 0.8 mM p-chloromercuribenzoate and by 1 mM N-ethylmaleimide, while only 17% and 23% inhibitions are observed with P-2, respectively. Ethanol inhibits the reaction with polymerase C and P-1, but stimulates P-2 reaction. The pH optimum of polymerase C is 7.0 in potassium phosphate buffer and that of P-1 is 6.3 in potassium phosphate, 7.3 in Tris-HCl, and 8.5 in glycine-KOH buffer. The pH optimum of P-2 is 9.8 in glycine-KOH buffer. Native DNA is more effective than heat-denatured DNA as a template for three polymerases, but activated DNA is far more effective than native DNA. Digestion of activated DNA with exonuclease III results in increases of template activity for polymerase C and P-1, but the increase with P-1 is very small. While for P-2 polymerase, no stimulating effect was observed. Poly[d(A-T) . poly[d(T-A)] is more effective than activated DNA for P-2 enzyme. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tsuruo, T. oth Ukita, T. oth in BBA Section Nucleic Acids And Protein Synthesis Amsterdam : Elsevier 353(1974), 2, Seite 146-159 (DE-627)NLEJ185870457 (DE-600)2209441-6 0005-2787 nnns volume:353 year:1974 number:2 pages:146-159 http://linkinghub.elsevier.com/retrieve/pii/0005-2787(74)90181-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 353 1974 2 146-159 |
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(DE-627)NLEJ185894097 (DE-599)GBVNLZ185894097 DE-627 ger DE-627 rakwb eng Purification and further characterization of three DNA polymerases of rat ascites hepatoma cells 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Three DNA polymerases have been isolated from rat ascites hepatoma cells and the properties of the reactions have been investigated. A polymerase (cytoplasmic polymerase: polymerase C) has been purified 560-fold from the soluble fraction of the cells and two different DNA polymerases (polymerase P-1 and P-2) have been purified about 70- and 60-fold, respectively, from the nuclear membrane chromatin fraction of the cells. Polymerase C has a low level of exonuclease activity but both preparations of P-1 and P-2 have no detectable nuclease activity.ATP stimulates DNA synthesis by nuclei and nuclear membrane chromatin fraction but has no stimulating effect on the purified polymerases. The activities of polymerase C and P-1 are strongly inhibited by 0.8 mM p-chloromercuribenzoate and by 1 mM N-ethylmaleimide, while only 17% and 23% inhibitions are observed with P-2, respectively. Ethanol inhibits the reaction with polymerase C and P-1, but stimulates P-2 reaction. The pH optimum of polymerase C is 7.0 in potassium phosphate buffer and that of P-1 is 6.3 in potassium phosphate, 7.3 in Tris-HCl, and 8.5 in glycine-KOH buffer. The pH optimum of P-2 is 9.8 in glycine-KOH buffer. Native DNA is more effective than heat-denatured DNA as a template for three polymerases, but activated DNA is far more effective than native DNA. Digestion of activated DNA with exonuclease III results in increases of template activity for polymerase C and P-1, but the increase with P-1 is very small. While for P-2 polymerase, no stimulating effect was observed. Poly[d(A-T) . poly[d(T-A)] is more effective than activated DNA for P-2 enzyme. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tsuruo, T. oth Ukita, T. oth in BBA Section Nucleic Acids And Protein Synthesis Amsterdam : Elsevier 353(1974), 2, Seite 146-159 (DE-627)NLEJ185870457 (DE-600)2209441-6 0005-2787 nnns volume:353 year:1974 number:2 pages:146-159 http://linkinghub.elsevier.com/retrieve/pii/0005-2787(74)90181-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 353 1974 2 146-159 |
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(DE-627)NLEJ185894097 (DE-599)GBVNLZ185894097 DE-627 ger DE-627 rakwb eng Purification and further characterization of three DNA polymerases of rat ascites hepatoma cells 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Three DNA polymerases have been isolated from rat ascites hepatoma cells and the properties of the reactions have been investigated. A polymerase (cytoplasmic polymerase: polymerase C) has been purified 560-fold from the soluble fraction of the cells and two different DNA polymerases (polymerase P-1 and P-2) have been purified about 70- and 60-fold, respectively, from the nuclear membrane chromatin fraction of the cells. Polymerase C has a low level of exonuclease activity but both preparations of P-1 and P-2 have no detectable nuclease activity.ATP stimulates DNA synthesis by nuclei and nuclear membrane chromatin fraction but has no stimulating effect on the purified polymerases. The activities of polymerase C and P-1 are strongly inhibited by 0.8 mM p-chloromercuribenzoate and by 1 mM N-ethylmaleimide, while only 17% and 23% inhibitions are observed with P-2, respectively. Ethanol inhibits the reaction with polymerase C and P-1, but stimulates P-2 reaction. The pH optimum of polymerase C is 7.0 in potassium phosphate buffer and that of P-1 is 6.3 in potassium phosphate, 7.3 in Tris-HCl, and 8.5 in glycine-KOH buffer. The pH optimum of P-2 is 9.8 in glycine-KOH buffer. Native DNA is more effective than heat-denatured DNA as a template for three polymerases, but activated DNA is far more effective than native DNA. Digestion of activated DNA with exonuclease III results in increases of template activity for polymerase C and P-1, but the increase with P-1 is very small. While for P-2 polymerase, no stimulating effect was observed. Poly[d(A-T) . poly[d(T-A)] is more effective than activated DNA for P-2 enzyme. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tsuruo, T. oth Ukita, T. oth in BBA Section Nucleic Acids And Protein Synthesis Amsterdam : Elsevier 353(1974), 2, Seite 146-159 (DE-627)NLEJ185870457 (DE-600)2209441-6 0005-2787 nnns volume:353 year:1974 number:2 pages:146-159 http://linkinghub.elsevier.com/retrieve/pii/0005-2787(74)90181-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 353 1974 2 146-159 |
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(DE-627)NLEJ185894097 (DE-599)GBVNLZ185894097 DE-627 ger DE-627 rakwb eng Purification and further characterization of three DNA polymerases of rat ascites hepatoma cells 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Three DNA polymerases have been isolated from rat ascites hepatoma cells and the properties of the reactions have been investigated. A polymerase (cytoplasmic polymerase: polymerase C) has been purified 560-fold from the soluble fraction of the cells and two different DNA polymerases (polymerase P-1 and P-2) have been purified about 70- and 60-fold, respectively, from the nuclear membrane chromatin fraction of the cells. Polymerase C has a low level of exonuclease activity but both preparations of P-1 and P-2 have no detectable nuclease activity.ATP stimulates DNA synthesis by nuclei and nuclear membrane chromatin fraction but has no stimulating effect on the purified polymerases. The activities of polymerase C and P-1 are strongly inhibited by 0.8 mM p-chloromercuribenzoate and by 1 mM N-ethylmaleimide, while only 17% and 23% inhibitions are observed with P-2, respectively. Ethanol inhibits the reaction with polymerase C and P-1, but stimulates P-2 reaction. The pH optimum of polymerase C is 7.0 in potassium phosphate buffer and that of P-1 is 6.3 in potassium phosphate, 7.3 in Tris-HCl, and 8.5 in glycine-KOH buffer. The pH optimum of P-2 is 9.8 in glycine-KOH buffer. Native DNA is more effective than heat-denatured DNA as a template for three polymerases, but activated DNA is far more effective than native DNA. Digestion of activated DNA with exonuclease III results in increases of template activity for polymerase C and P-1, but the increase with P-1 is very small. While for P-2 polymerase, no stimulating effect was observed. Poly[d(A-T) . poly[d(T-A)] is more effective than activated DNA for P-2 enzyme. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tsuruo, T. oth Ukita, T. oth in BBA Section Nucleic Acids And Protein Synthesis Amsterdam : Elsevier 353(1974), 2, Seite 146-159 (DE-627)NLEJ185870457 (DE-600)2209441-6 0005-2787 nnns volume:353 year:1974 number:2 pages:146-159 http://linkinghub.elsevier.com/retrieve/pii/0005-2787(74)90181-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 353 1974 2 146-159 |
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(DE-627)NLEJ185894097 (DE-599)GBVNLZ185894097 DE-627 ger DE-627 rakwb eng Purification and further characterization of three DNA polymerases of rat ascites hepatoma cells 1974 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Three DNA polymerases have been isolated from rat ascites hepatoma cells and the properties of the reactions have been investigated. A polymerase (cytoplasmic polymerase: polymerase C) has been purified 560-fold from the soluble fraction of the cells and two different DNA polymerases (polymerase P-1 and P-2) have been purified about 70- and 60-fold, respectively, from the nuclear membrane chromatin fraction of the cells. Polymerase C has a low level of exonuclease activity but both preparations of P-1 and P-2 have no detectable nuclease activity.ATP stimulates DNA synthesis by nuclei and nuclear membrane chromatin fraction but has no stimulating effect on the purified polymerases. The activities of polymerase C and P-1 are strongly inhibited by 0.8 mM p-chloromercuribenzoate and by 1 mM N-ethylmaleimide, while only 17% and 23% inhibitions are observed with P-2, respectively. Ethanol inhibits the reaction with polymerase C and P-1, but stimulates P-2 reaction. The pH optimum of polymerase C is 7.0 in potassium phosphate buffer and that of P-1 is 6.3 in potassium phosphate, 7.3 in Tris-HCl, and 8.5 in glycine-KOH buffer. The pH optimum of P-2 is 9.8 in glycine-KOH buffer. Native DNA is more effective than heat-denatured DNA as a template for three polymerases, but activated DNA is far more effective than native DNA. Digestion of activated DNA with exonuclease III results in increases of template activity for polymerase C and P-1, but the increase with P-1 is very small. While for P-2 polymerase, no stimulating effect was observed. Poly[d(A-T) . poly[d(T-A)] is more effective than activated DNA for P-2 enzyme. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Tsuruo, T. oth Ukita, T. oth in BBA Section Nucleic Acids And Protein Synthesis Amsterdam : Elsevier 353(1974), 2, Seite 146-159 (DE-627)NLEJ185870457 (DE-600)2209441-6 0005-2787 nnns volume:353 year:1974 number:2 pages:146-159 http://linkinghub.elsevier.com/retrieve/pii/0005-2787(74)90181-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 353 1974 2 146-159 |
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Purification and further characterization of three DNA polymerases of rat ascites hepatoma cells |
| abstract |
Three DNA polymerases have been isolated from rat ascites hepatoma cells and the properties of the reactions have been investigated. A polymerase (cytoplasmic polymerase: polymerase C) has been purified 560-fold from the soluble fraction of the cells and two different DNA polymerases (polymerase P-1 and P-2) have been purified about 70- and 60-fold, respectively, from the nuclear membrane chromatin fraction of the cells. Polymerase C has a low level of exonuclease activity but both preparations of P-1 and P-2 have no detectable nuclease activity.ATP stimulates DNA synthesis by nuclei and nuclear membrane chromatin fraction but has no stimulating effect on the purified polymerases. The activities of polymerase C and P-1 are strongly inhibited by 0.8 mM p-chloromercuribenzoate and by 1 mM N-ethylmaleimide, while only 17% and 23% inhibitions are observed with P-2, respectively. Ethanol inhibits the reaction with polymerase C and P-1, but stimulates P-2 reaction. The pH optimum of polymerase C is 7.0 in potassium phosphate buffer and that of P-1 is 6.3 in potassium phosphate, 7.3 in Tris-HCl, and 8.5 in glycine-KOH buffer. The pH optimum of P-2 is 9.8 in glycine-KOH buffer. Native DNA is more effective than heat-denatured DNA as a template for three polymerases, but activated DNA is far more effective than native DNA. Digestion of activated DNA with exonuclease III results in increases of template activity for polymerase C and P-1, but the increase with P-1 is very small. While for P-2 polymerase, no stimulating effect was observed. Poly[d(A-T) . poly[d(T-A)] is more effective than activated DNA for P-2 enzyme. |
| abstractGer |
Three DNA polymerases have been isolated from rat ascites hepatoma cells and the properties of the reactions have been investigated. A polymerase (cytoplasmic polymerase: polymerase C) has been purified 560-fold from the soluble fraction of the cells and two different DNA polymerases (polymerase P-1 and P-2) have been purified about 70- and 60-fold, respectively, from the nuclear membrane chromatin fraction of the cells. Polymerase C has a low level of exonuclease activity but both preparations of P-1 and P-2 have no detectable nuclease activity.ATP stimulates DNA synthesis by nuclei and nuclear membrane chromatin fraction but has no stimulating effect on the purified polymerases. The activities of polymerase C and P-1 are strongly inhibited by 0.8 mM p-chloromercuribenzoate and by 1 mM N-ethylmaleimide, while only 17% and 23% inhibitions are observed with P-2, respectively. Ethanol inhibits the reaction with polymerase C and P-1, but stimulates P-2 reaction. The pH optimum of polymerase C is 7.0 in potassium phosphate buffer and that of P-1 is 6.3 in potassium phosphate, 7.3 in Tris-HCl, and 8.5 in glycine-KOH buffer. The pH optimum of P-2 is 9.8 in glycine-KOH buffer. Native DNA is more effective than heat-denatured DNA as a template for three polymerases, but activated DNA is far more effective than native DNA. Digestion of activated DNA with exonuclease III results in increases of template activity for polymerase C and P-1, but the increase with P-1 is very small. While for P-2 polymerase, no stimulating effect was observed. Poly[d(A-T) . poly[d(T-A)] is more effective than activated DNA for P-2 enzyme. |
| abstract_unstemmed |
Three DNA polymerases have been isolated from rat ascites hepatoma cells and the properties of the reactions have been investigated. A polymerase (cytoplasmic polymerase: polymerase C) has been purified 560-fold from the soluble fraction of the cells and two different DNA polymerases (polymerase P-1 and P-2) have been purified about 70- and 60-fold, respectively, from the nuclear membrane chromatin fraction of the cells. Polymerase C has a low level of exonuclease activity but both preparations of P-1 and P-2 have no detectable nuclease activity.ATP stimulates DNA synthesis by nuclei and nuclear membrane chromatin fraction but has no stimulating effect on the purified polymerases. The activities of polymerase C and P-1 are strongly inhibited by 0.8 mM p-chloromercuribenzoate and by 1 mM N-ethylmaleimide, while only 17% and 23% inhibitions are observed with P-2, respectively. Ethanol inhibits the reaction with polymerase C and P-1, but stimulates P-2 reaction. The pH optimum of polymerase C is 7.0 in potassium phosphate buffer and that of P-1 is 6.3 in potassium phosphate, 7.3 in Tris-HCl, and 8.5 in glycine-KOH buffer. The pH optimum of P-2 is 9.8 in glycine-KOH buffer. Native DNA is more effective than heat-denatured DNA as a template for three polymerases, but activated DNA is far more effective than native DNA. Digestion of activated DNA with exonuclease III results in increases of template activity for polymerase C and P-1, but the increase with P-1 is very small. While for P-2 polymerase, no stimulating effect was observed. Poly[d(A-T) . poly[d(T-A)] is more effective than activated DNA for P-2 enzyme. |
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Purification and further characterization of three DNA polymerases of rat ascites hepatoma cells |
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