Results 271 to 280 of about 22,541 (295)
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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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Cellular and Molecular Life Sciences (CMLS), 1998
The eosinophil ribonucleases, eosinophilderived neurotoxin (EDN/RNase 2) and eosinophil cationic protein (ECP/RNase 3) are two closely related proteins with intriguing functional and evolutionary properties. While both EDN and ECP maintain the structural and catalytic residues typical of the RNase A superfamily, the role of ribonuclease activity in the
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The eosinophil ribonucleases, eosinophilderived neurotoxin (EDN/RNase 2) and eosinophil cationic protein (ECP/RNase 3) are two closely related proteins with intriguing functional and evolutionary properties. While both EDN and ECP maintain the structural and catalytic residues typical of the RNase A superfamily, the role of ribonuclease activity in the
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Current Protocols in Molecular Biology, 1993
AbstractSequence‐specific hybridization probes of high specific activity are prepared by cloning the probe sequence downstream of a bacteriophage promoter. The plasmid is cleaved with a restriction enzyme, and the plasmid DNA is transcribed with bacteriophage RNA polymerase, which efficiently transcribes the cloned sequence into a discrete RNA species ...
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AbstractSequence‐specific hybridization probes of high specific activity are prepared by cloning the probe sequence downstream of a bacteriophage promoter. The plasmid is cleaved with a restriction enzyme, and the plasmid DNA is transcribed with bacteriophage RNA polymerase, which efficiently transcribes the cloned sequence into a discrete RNA species ...
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