Results 261 to 270 of about 132,332 (305)
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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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Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1967
Abstract 1. 1. A ribonuclease from bovine aorta has been partially purified. 2. 2. The purification procedure involved ethanol fractionation and gel filtration on polyacrylamide and Sephadex. 3. 3. The enzyme is free of deoxyribonuclease, phosphomonoesterase, and cyclic phosphatase activity (under the conditions employed).
W, Gamble, G H, Nayar, E S, Kiersky
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Abstract 1. 1. A ribonuclease from bovine aorta has been partially purified. 2. 2. The purification procedure involved ethanol fractionation and gel filtration on polyacrylamide and Sephadex. 3. 3. The enzyme is free of deoxyribonuclease, phosphomonoesterase, and cyclic phosphatase activity (under the conditions employed).
W, Gamble, G H, Nayar, E S, Kiersky
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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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Human granulocyte ribonuclease
Biochemical and Biophysical Research Communications, 1976Abstract Human granulocytes contain an RNase which is thermostable at pH 4.2 and thermolabile at pH 8.5. It has a pH optimum at 6.5. It exhibits highest preference for the secondary phosphate esters of uridine 3′-phosphates. It has no action on uridine 2′: 3′-cyclic phosphates. Poly (A) and poly (G) are inert to its action.
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Experientia, 1947
L'activite de la ribonuclease vis-a-vis des ribonucleoproteides de la levure est inhibee par la penicilline.
L, MASSART, G, PEETERS, A, VANHOUCKE
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L'activite de la ribonuclease vis-a-vis des ribonucleoproteides de la levure est inhibee par la penicilline.
L, MASSART, G, PEETERS, A, VANHOUCKE
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Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
Two components having ribonuclease (EC 3.1.27.5) activity were isolated from human milk. Each component of human milk ribonuclease (RNAase) moved at a slightly different rate when electrophoresed on polyacrylamide gel but at the same rate when ultracentrifuged. The major component had a molecular weight of approx. 14 000, an isoelectric point of pH 7.9,
B K, Dalaly +3 more
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Two components having ribonuclease (EC 3.1.27.5) activity were isolated from human milk. Each component of human milk ribonuclease (RNAase) moved at a slightly different rate when electrophoresed on polyacrylamide gel but at the same rate when ultracentrifuged. The major component had a molecular weight of approx. 14 000, an isoelectric point of pH 7.9,
B K, Dalaly +3 more
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Biochemical and Biophysical Research Communications, 1977
Abstract Human platelets contain an RNase which has a pH optimum at 5.0. It hydrolyzes the secondary phosphate esters of uridine 3′-phosphates. It slowly converts uridine 2′:3′-and cytidine 2′:3′-cyclic phosphates to their corresponding nucleoside 3′-phosphates. Poly (A), poly (G) and poly (C) are not only refractory to the action of this enzyme, but
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Abstract Human platelets contain an RNase which has a pH optimum at 5.0. It hydrolyzes the secondary phosphate esters of uridine 3′-phosphates. It slowly converts uridine 2′:3′-and cytidine 2′:3′-cyclic phosphates to their corresponding nucleoside 3′-phosphates. Poly (A), poly (G) and poly (C) are not only refractory to the action of this enzyme, but
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2001
Publisher Summary This chapter describes methods and approaches to purify and characterize polysomal ribonuclease 1 (PMR-1). It is the first mRNA endoribonuclease to be purified and cloned. Because PMR-1 was found in association with mRNA-containing complexes, the first steps in its analysis required facile approaches for the isolation of messenger ...
K S, Cunningham +2 more
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Publisher Summary This chapter describes methods and approaches to purify and characterize polysomal ribonuclease 1 (PMR-1). It is the first mRNA endoribonuclease to be purified and cloned. Because PMR-1 was found in association with mRNA-containing complexes, the first steps in its analysis required facile approaches for the isolation of messenger ...
K S, Cunningham +2 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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2001
Publisher Summary Ribonuclease P is a ribonucleoprotein nuclease required for the site-specific cleavage of the 5′ leader sequence of precursor tRNAs. In eubacteria, the RNA subunit of RNase P is the catalytic moiety and is capable of processing precursor tRNA in the presence of divalent metal ions.
N, Jarrous, S, Altman
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Publisher Summary Ribonuclease P is a ribonucleoprotein nuclease required for the site-specific cleavage of the 5′ leader sequence of precursor tRNAs. In eubacteria, the RNA subunit of RNase P is the catalytic moiety and is capable of processing precursor tRNA in the presence of divalent metal ions.
N, Jarrous, S, Altman
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