Results 271 to 280 of about 21,043 (311)
Some of the next articles are maybe not open access.
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.
openaire +2 more sources
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
openaire +2 more sources
L'activite de la ribonuclease vis-a-vis des ribonucleoproteides de la levure est inhibee par la penicilline.
L, MASSART, G, PEETERS, A, VANHOUCKE
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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][
openaire +2 more sources
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][
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +2 more sources
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 ...
openaire +3 more sources
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 ...
openaire +3 more sources