Results 221 to 230 of about 34,862 (253)
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Journal of Molecular Biology, 1981
A strain of Escherichia coli lacking RNAase III and containing thermolabile RNAase E and RNAase P was labeled with 32Pi at a non-permissive temperature. RNA molecules were separated by two-dimensional polyacrylamide gel electrophoresis. Most of the small RNA species were isolated and analyzed for the presence of 5′ nucleoside triphosphates.
G, Plautz, D, Apirion
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A strain of Escherichia coli lacking RNAase III and containing thermolabile RNAase E and RNAase P was labeled with 32Pi at a non-permissive temperature. RNA molecules were separated by two-dimensional polyacrylamide gel electrophoresis. Most of the small RNA species were isolated and analyzed for the presence of 5′ nucleoside triphosphates.
G, Plautz, D, Apirion
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Inhibitiory effects of gold(III) ions on ribonuclease and deoxyribonuclease
Journal of Inorganic Biochemistry, 2007Inhibitory effects of gold(III) ions (Au(III)) on ribonuclease A (RNase A) and deoxyribonuclease I (DNase I) were investigated at neutral pH. RNase A was completely inhibited by 3 molar equivalents of Au(III) ions. DNase I was inhibited by 10 molar equivalents of Au(III) ions.
Tatsuo, Maruyama +3 more
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Processing of bacteriophage T4 primary transcripts with ribonuclease III
Journal of Molecular Biology, 1982Abstract The two promoters (P 1 and P 2 ) of the cluster of transfer RNA genes of bacteriophage T4 are situated at distances of 0.95 × 10 3 and 1.3 × 10 3 bases, respectively, from the first tRNA gene. Isolated in vitro primary transcripts initiated at these promoters were incubated with highly purified RNase III. The resulting cleavage products
T, Barkay, A, Goldfarb
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Consequences of losing ribonuclease III on theEscherichia coli cell
Molecular and General Genetics MGG, 1976An isogenic pair of Escherichia coli strains, one carrying an rnc+ and the other an rnc- allele (a mutation which reduces the level of ribonuclease III), was compared. The rnc- strain fails to grow at very elevated temperatures (for E. coli) while the rnc+ strain does grow exponentially.
D, Apirion, J, Neil, N, Watson
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Escherichia coli ribonuclease III
1990Publisher Summary This chapter considers methods for the assay of RNase III, preparation of the substrates required, and a purification scheme for the enzyme that has been tested on strains of E. coli carrying cloned copies of the gene for RNase III (the rnc gene), which has recently been identified and sequenced.
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1982
Publisher Summary Ribonuclease III (RNase III) of Escherichia coli is responsible for the first steps in the post-transcriptional processing of E. coli ribosomal RNA. RNase III was first characterized as an endoribonuclease that specifically degrades double-stranded RNAs of either natural or synthetic origin.
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Publisher Summary Ribonuclease III (RNase III) of Escherichia coli is responsible for the first steps in the post-transcriptional processing of E. coli ribosomal RNA. RNase III was first characterized as an endoribonuclease that specifically degrades double-stranded RNAs of either natural or synthetic origin.
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Biochimica et Biophysica Acta (BBA) - Specialized Section on Nucleic Acids and Related Subjects, 1962
Abstract The specific activities of total alkaline RNAase, total acid RNAase and free RNAase inhibitor have been followed during the regeneration of rat liver induced by partial hepatectomy. A significant increase in the level of RNAase inhibitor occurred within 12 h of operation and a maximum increase (39%) was observed after 48h.
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Abstract The specific activities of total alkaline RNAase, total acid RNAase and free RNAase inhibitor have been followed during the regeneration of rat liver induced by partial hepatectomy. A significant increase in the level of RNAase inhibitor occurred within 12 h of operation and a maximum increase (39%) was observed after 48h.
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Biochemical properties of Bacillus Calmette Guerin ribonuclease III
Journal of Basic Microbiology, 2015Double‐stranded RNA (dsRNA) is discovered to participate in the regulation of gene expression in both bacterial and eukaryotic cells. Members of ribonuclease III (RNase III) family recognize RNA motifs and cleave substrates at specific sites in a divalent‐metal‐ion‐dependent manner.
Lei, Yang +5 more
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The Ribonuclease of Phaseolus Aureus Roxb: III. — Effectors and Specificity
Archives Internationales de Physiologie et de Biochimie, 1961AbstractSeveral divalent metal ions (Hg++, Cu++, Zn++ are powerful inhibitors of the Phaseolus aureus RNase activity. Other divalent metal ions inhibit less; none of those investigated activate the enzyme.Anionic polymers do not inhibit in conditions where they are very effective against pancreatic RNase. This is the case for heparin, sulphated pectins
J, STOCKX, L, VANDENDRIESSCHE
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The action of ribonuclease of neoplastic growth III. Studies by interference microscopy
Biochimica et Biophysica Acta, 1956Abstract The action of ribonuclease, in vitro, on a number of suspensions of living ascites cells, in different physiological conditions, has been followed and measured by interference microscopy. The results show that ribonuclease can produce an important initial increase in the cellular mass (biochemical estimations, made in parallel, indicate ...
D M, EASTY, L, LEDOUX, E J, AMBROSE
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