Results 351 to 360 of about 156,401 (384)
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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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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.
Keith Breese, Henry B. Bull
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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.
Keith Breese, Henry B. Bull
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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.
Kimiko Sato-Asano +3 more
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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.
Kimiko Sato-Asano +3 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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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
S J Morris +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
S J Morris +7 more
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Experientia, 1947
L'activite de la ribonuclease vis-a-vis des ribonucleoproteides de la levure est inhibee par la penicilline.
A Vanhoucke, L. Massart, G. Peeters
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L'activite de la ribonuclease vis-a-vis des ribonucleoproteides de la levure est inhibee par la penicilline.
A Vanhoucke, L. Massart, G. Peeters
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Luminescence of ribonuclease A
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1971Abstract The effect of disulfide bonds on the phosphorescence properties of tyrosyl residues of model compounds and ribonuclease A was investigated. 1. 1.|The tyrosyl residues of polytyrosine, insulin heptapeptide, lysine-tyrosine copolymer, and cysteinyltyrosine are characterized by luminescence ratios ( q P q F ) which are ...
John E. Wampler, Jorge E. Churchich
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Cytotoxicity of Polyspermine-Ribonuclease A and Polyspermine-Dimeric Ribonuclease A
Bioconjugate Chemistry, 2007Polyspermine-ribonuclease A (PS-RNase A) and polyspermine-dimeric ribonuclease A (PS-dimeric RNase A) were prepared by cross-linking ribonuclease A or its covalently linked dimer to polyspermine (PS) using dimethyl suberimidate. The two RNase A derivatives were tested for a possible antitumor action.
P. POUCKOVA +9 more
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Science, 2002
In the recent review by S. A. Benner et al. (“Planetary biology—paleontological, geological, and molecular histories of life,” 3 May, p. [864][1]), Fig. 4 shows an evolutionary tree, which was previously published by the authors ([1][2]) and which was reproduced from a 1986 paper of ours ([2][
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In the recent review by S. A. Benner et al. (“Planetary biology—paleontological, geological, and molecular histories of life,” 3 May, p. [864][1]), Fig. 4 shows an evolutionary tree, which was previously published by the authors ([1][2]) and which was reproduced from a 1986 paper of ours ([2][
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