Results 251 to 260 of about 14,217 (304)
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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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Ribonuclease and ribonuclease inhibitor in the human pancreas
Gastroenterologia Japonica, 1983Previous investigations have failed to confirm any specificity of elevated serum ribonuclease (RNase) in the diagnosis of pancreatic cancer. Although RNase had been known to be present in two forms (free and inhibitor-bound) in various rat tissues, little was known about its presence in the human pancreas. This report investigates the presence of RNase
H, Kiyohara, M, Menjo
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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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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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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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Archives of Biochemistry and Biophysics, 1965
Abstract The titration of ribonuclease, acid to its isoionic point, has been conducted in 1.80 M KCl. The slopes of the titration curves in the neighborhood of half neutralization of the carboxyl groups have been studied at several ionic strengths.
H B, BULL, K, BREESE
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Abstract The titration of ribonuclease, acid to its isoionic point, has been conducted in 1.80 M KCl. The slopes of the titration curves in the neighborhood of half neutralization of the carboxyl groups have been studied at several ionic strengths.
H B, BULL, K, BREESE
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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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Nature, 1967
A 5.5 A electron density map of ribonuclease has been obtained by X-ray diffraction using five isomorphous derivatives. One of the cystine residues is identified by means of a chemically modified protein and, using this residue as a starting point, likely positions are found for the other three. Using 2′-cytidylic acid as an inhibitor the active region
H P, Avey +7 more
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A 5.5 A electron density map of ribonuclease has been obtained by X-ray diffraction using five isomorphous derivatives. One of the cystine residues is identified by means of a chemically modified protein and, using this residue as a starting point, likely positions are found for the other three. Using 2′-cytidylic acid as an inhibitor the active region
H P, Avey +7 more
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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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