Results 251 to 260 of about 132,332 (305)
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Current Protocols in Molecular Biology, 2008
AbstractRibonucleases (RNases) with different sequence or structural specificities are used for a variety of analytical purposes, including RNA sequencing, mapping, and quantitation. The development of RNase protection assays, structural determination assays, and the production of small interfering RNAs (siRNA) employed in RNA interference (RNAi ...
Nicole M, Nichols, Dongxian, Yue
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AbstractRibonucleases (RNases) with different sequence or structural specificities are used for a variety of analytical purposes, including RNA sequencing, mapping, and quantitation. The development of RNase protection assays, structural determination assays, and the production of small interfering RNAs (siRNA) employed in RNA interference (RNAi ...
Nicole M, Nichols, Dongxian, Yue
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Org. Biomol. Chem., 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Teija, Niittymäki, Harri, Lönnberg
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AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
Teija, Niittymäki, Harri, Lönnberg
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Current Protocols in Molecular Biology, 1989
AbstractRibonucleases (RNases) with different sequence specificities are used for a variety of analytical purposes, including RNA sequencing, mapping, and quantitation. One very common application for RNase A is presented in this unit and involves hydrolyzing RNA that contaminates DNA preparations.
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AbstractRibonucleases (RNases) with different sequence specificities are used for a variety of analytical purposes, including RNA sequencing, mapping, and quantitation. One very common application for RNase A is presented in this unit and involves hydrolyzing RNA that contaminates DNA preparations.
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2002
The ribonuclease protection assay (RPA) is a sensitive technique for the analysis of total cellular RNA. It involves generating a specific antisense riboprobe, hybridizing the probe to total RNA, removing unprotected RNA by RNases, and finally isolating and analyzing the protected RNA on a denaturing gel.
J L, Thorvaldsen, M S, Bartolomei
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The ribonuclease protection assay (RPA) is a sensitive technique for the analysis of total cellular RNA. It involves generating a specific antisense riboprobe, hybridizing the probe to total RNA, removing unprotected RNA by RNases, and finally isolating and analyzing the protected RNA on a denaturing gel.
J L, Thorvaldsen, M S, Bartolomei
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Ribonuclease IX. Further studies on ribonuclease inhibitor
Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects, 1962Abstract Ribonuclease inhibitor was found in the livers of five mammalian species, but could not be detected in the liver of chicken or frog. Detailed examination of the ribonuclease activity of chicken-liver homogenate and various subcellular fractions under different conditions failed to provide convincing evidence for the presence of an inhibitor ...
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Ribonuclease. II. Activators and inhibitors for ribonuclease
Archives of Biochemistry and Biophysics, 1953Abstract Heparin and treburon, a synthetic heparin-like polysaccharide, inhibit pancreatic ribonuclease and ribonuclease activity in rat kidney and liver. Pancreatic desoxyribonuclease is inhibited to a lesser extent. The inhibition appears to be a competitive one between the acid polysaccharide and RNA or DNA.
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Biochimica et Biophysica Acta (BBA) - Protein Structure, 1968
Abstract The nitration of bovine pancreatic ribonuclease with tetranitromethane has been studied. A procedure involving solvent extraction of excess reagent and product is described. A spectrophotometric procedure for determining the extent of nitration of tyrosines has been devised, which is not vitiated by the presence of other chromophoric ...
G H, Beaven, W B, Gratzer
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Abstract The nitration of bovine pancreatic ribonuclease with tetranitromethane has been studied. A procedure involving solvent extraction of excess reagent and product is described. A spectrophotometric procedure for determining the extent of nitration of tyrosines has been devised, which is not vitiated by the presence of other chromophoric ...
G H, Beaven, W B, Gratzer
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Planta, 1972
1. Ribonuclease (RNase) activity in styles with conducting tissue is about 20 times higher than that of open styles with a stylar canal. 2. RNase activity is localized in or between the cells of the conducting tissue. 3. Activity is not influenced by pollination. 4. Stylar RNase has a temperature optimum at 45°C and a pH optimum at pH 6.5.
J, Schrauwen, H F, Linskens
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1. Ribonuclease (RNase) activity in styles with conducting tissue is about 20 times higher than that of open styles with a stylar canal. 2. RNase activity is localized in or between the cells of the conducting tissue. 3. Activity is not influenced by pollination. 4. Stylar RNase has a temperature optimum at 45°C and a pH optimum at pH 6.5.
J, Schrauwen, H F, Linskens
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Biochimica et Biophysica Acta (BBA) - Enzymology, 1969
Abstract Rat serum ribonuclease has been purified about 6000-fold. The optimal pH of this enzyme was 7–8. The purified enzyme was rather heat labile at pH 7.6. The Km of this enzyme is 30% higher than that of the crystalline bovine pancreatic ribonuclease (polyribonucleotide 2-oligonucleotide-transferase, EC 2.7.7.16).
T, Umeda +3 more
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Abstract Rat serum ribonuclease has been purified about 6000-fold. The optimal pH of this enzyme was 7–8. The purified enzyme was rather heat labile at pH 7.6. The Km of this enzyme is 30% higher than that of the crystalline bovine pancreatic ribonuclease (polyribonucleotide 2-oligonucleotide-transferase, EC 2.7.7.16).
T, Umeda +3 more
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Nature, 1960
THE existence of a thermostable ribonuclease in commercial takadiastase was first pointed by Kuninaka1. We found afterwards by zone-electrophoresis the existence of at least three enzymes attacking ribonucleic acid in takadiastase: one of them is more active at pH 7.5 and the others are more active at pH 4.5 2.
K, SATO-ASANO, F, EGAMI
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THE existence of a thermostable ribonuclease in commercial takadiastase was first pointed by Kuninaka1. We found afterwards by zone-electrophoresis the existence of at least three enzymes attacking ribonucleic acid in takadiastase: one of them is more active at pH 7.5 and the others are more active at pH 4.5 2.
K, SATO-ASANO, F, EGAMI
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