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At least 199 records · Page 11Linked to original sources
PubMed1978

Soluble endoribonuclease activity from vaccinia virus: specific cleavage of virion-associated high-molecular-weight RNA.

A soluble endoribonuclease activity was extracted from purified vaccinia virus cores by treatment with sodium-deoxycholate and dithiothreitol. The soluble enzyme readily cleaved purified virion-associated high-molecular-weight RNA to limit-sized fragments sedimenting at 8 to 12S. Purified virion-released 8 to 12S polyadenylated mRNA was not degraded by the enzyme extract. The soluble endoribonuclease did not require the presence of ribonucleoside triphosphates for activity.

Endonucleases↗
PubMed1982

[Analysis of soluble nuclear fractions regulating RNA synthesis].

The influence of the rat liver nuclear extract on RNA synthesis in the system of isolated cell nuclei of the rat liver was investigated. Two factors were discovered with opposite influence on RNA synthesis: one stimulating, while the other inhibiting the synthesis. A fraction of high-polymeric RNA (7-9 S) and a fraction of the total protein were isolated from the extract. The influence of these fractions on the transcription process was studied both in isolated nuclei and in the system containing pure liver DNA in the presence of RNA polymerase of E. coli. In both the cases the total fraction of protein turned out to stimulate RNA synthesis, while the high-polymeric fraction of RNA inhibited it. The soluble fractions, detected in the cells and influencing RNA synthesis, interact with RNA polymerase either increasing or decreasing the activity of the enzyme.

Animals↗
PubMed1991

Purification of RNA using an anti-RNA monoclonal antibody.

Studies of the synthesis and modification of RNA employ many types of in vitro reactions. Often, the RNA product must be concentrated or purified away from other reaction components such as salts, unincorporated nucleotides, protein, or DNA. Here I describe an immunological approach suitable for the isolation of RNA from in vitro reactions. A variety of RNAs of differing size and nucleotide sequence were immunoprecipitated with a monoclonal antibody specific for RNA. RNA binding took place in seconds with nearly quantitative recoveries. Immunoprecipitation was more efficient than ethanol precipitation in removing unincorporated nucleotides. Proteins which do not bind to RNA remained soluble. The immunoprecipitated RNA sample was solubilized directly with a buffered solution suitable for gel electrophoresis under denaturing conditions. Thus, RNAs can be rapidly concentrated for electrophoresis in a single step. Antibody-RNA binding was reversible under nondenaturing conditions in the presence of excess rRNA. This procedure serves as a novel means of purifying RNA and RNA-binding proteins from in vitro reactions.

Animals↗
PubMed1963

NUCLEOTIDE COMPOSITION OF RIBONUCLEIC ACID FROM NEUROSPORA CRASSA.

Henney, H. (The University of Texas, Austin) and R. Storck. Nucleotide composition of ribonucleic acid from Neurospora crassa. J. Bacteriol. 85:822-826. 1963.-The nucleotide composition of total, ribosomal, and soluble ribonucleic acid (RNA) from the conidia and the hyphae of Neurospora crassa was determined. The corresponding RNA classes from the two morphological types had the same base ratio. Total, ribosomal, and soluble RNA from hyphae contained, respectively, 51.0, 50.2, and 61.6% guanylic acid (G) plus cytidylic acid (C), and from conidia, 50.6, 49.9, and 62.1%. The proportion of nucleotides in ribosomal RNA was in close agreement with that reported for ribosomal RNA from other organisms. Soluble RNA contained 2.8% pseudouridylic acid, 36.0% C, and 25.5% G, and differed from soluble RNA from other sources in its high C content. Centrifugation of purified RNA from conidia and hyphae, through a linear sucrose-density gradient, yielded identical sedimentation profiles.

Neurospora↗
PubMed2004

Inhibition of angiogenesis in human glioma cell lines by antisense RNA from the soluble guanylate cyclase genes, GUCY1A3 and GUCY1B3.

Malignant gliomas, most of which show an elevated level of vascular endothelial cell growth factor (VEGF) expression, are well known for their hyper-vascularity. One of the possible inducers of VEGF in tumor cells is nitric oxide (NO), which is synthesized by NO synthase and stimulates soluble guanylate cyclase (GC) in tumor cells. Here, we report that 2 of 9 human glioma cell lines, CCF-STTG1 and U-87MG, overproduced cyclic GMP (cGMP) and showed increased expression of both or either subunits of soluble GC1, GUCY1A3 and GUCY1B3. Transfection of antisense GUCY1A3 or GUCY1B3 into these two glioma cell lines markedly reduced the content of cGMP and expression of VEGF. The angiogenic activity in vitro was subsequently inhibited, which was determined by induction of HUVEC cell growth. Furthermore, subcutaneous tumor formation by U-87MG cells in nude mice was dramatically suppressed to less than 0.05% in volume by transfection of either antisense GUCY1A3 or antisense GUCY1B3, which was accompanied by the significant decrease in vascular index to about 10%. These findings demonstrate that cGMP is an upstream mediator of VEGF expression in glioma cells and that soluble guanylate cyclases could be the target molecules for controlling neo-vascularization in a subset of human malignant gliomas.

Animals↗
PubMed1967

Purification and properties of methionyl-transfer-ribonucleic acid synthetase from Escherichia coli.

1. Methionyl-t-RNA synthetase (where t-RNA denotes ;soluble' or transfer RNA) has been purified to apparent homogeneity from a ribonuclease I-free strain of Escherichia coli. Polyacrylamide-gel electrophoresis of the final product revealed a single band. The purified enzyme catalyses the exchange of 450mumoles of pyrophosphate into ATP/mg. in 15min. at 37 degrees . 2. Methionyl-t-RNA synthetase is specific for the l-isomer of methionine, but appears to catalyse the methionylation of two distinct species of t-RNA, both of which are specific for methionine, but only one of which may be subsequently formylated. 3. The Michaelis constant for l-methionine is 2x10(-4)m in the ATP-PP(i) exchange assay and 2x10(-5)m for the acylation of t-RNA. 4. Gel filtration of both crude and highly purified preparations of methionyl-t-RNA synthetase on Sephadex G-200 indicates that the active species of enzyme has a molecular weight of about 190000. The amino acid composition of the enzyme is similar to those reported for the isoleucine and tyrosine enzymes from E. coli.

Adenosine Triphosphate↗