DNA polymerase activity associated with endogenous template: release by ribonuclease treatment. 1975

F Moranelli, and P E Penner

A ribonuclease-sensitive DNA polymerase, which uses an endogenous template, is detectable in the 39,000 g supernatant of a rat thymus homogenate, and appears as a single peak of activity in the void volume after Sephadex G 150 or G 200 gel filtration chromatography. Native and "activated" DNA-dependent DNA polymerase activities coincide with the endogenous-templated polymerase activity. Treatment of the thymus extract with ribonuclease(s) prior to gel filtration chromatography yields two other peaks of activity in addition to the void volume peak. The appearance of the two lower molecular weight peaks of activity is accompanied by a concomitant decrease in the endogenous-templated activity. The effect of ribonuclease is specific and cannot be reproduced by a similar deoxyribonuclease treatment.

UI MeSH Term Description Entries
D008274 Magnesium A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
D003854 Deoxyribonucleotides A purine or pyrimidine base bonded to a DEOXYRIBOSE containing a bond to a phosphate group. Deoxyribonucleotide
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D004254 DNA Nucleotidyltransferases Enzymes that catalyze the incorporation of deoxyribonucleotides into a chain of DNA. EC 2.7.7.-. Nucleotidyltransferases, DNA
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D005033 Ethylmaleimide A sulfhydryl reagent that is widely used in experimental biochemical studies. N-Ethylmaleimide,N Ethylmaleimide
D005260 Female Females
D006163 Ribonuclease T1 An enzyme catalyzing the endonucleolytic cleavage of RNA at the 3'-position of a guanylate residue. EC 3.1.27.3. Guanyloribonuclease,RNase T1,Ribonuclease N1,Aspergillus oryzae Ribonuclease,Guanyl-Specific RNase,RNase Apl,RNase F1,RNase Pch 1,RNase ST,Ribonuclease F1,Ribonuclease F2,Ribonuclease ST,Ribonuclease T-1,T 1 RNase,Guanyl Specific RNase,RNase, Guanyl-Specific,RNase, T 1,Ribonuclease T 1,Ribonuclease, Aspergillus oryzae
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012260 Ribonucleases Enzymes that catalyze the hydrolysis of ester bonds within RNA. EC 3.1.-. Nucleases, RNA,RNase,Acid Ribonuclease,Alkaline Ribonuclease,Ribonuclease,RNA Nucleases,Ribonuclease, Acid,Ribonuclease, Alkaline

Related Publications

F Moranelli, and P E Penner
April 1971, FEBS letters,
F Moranelli, and P E Penner
March 1971, Biochemical and biophysical research communications,
F Moranelli, and P E Penner
December 1974, Biochemical and biophysical research communications,
F Moranelli, and P E Penner
December 1977, The Journal of biological chemistry,
F Moranelli, and P E Penner
January 1973, Johns Hopkins medical journal. Supplement,
F Moranelli, and P E Penner
January 1984, Advances in experimental medicine and biology,
F Moranelli, and P E Penner
February 1972, Biochemical and biophysical research communications,
F Moranelli, and P E Penner
October 1968, Plant physiology,
Copied contents to your clipboard!