Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.27.4 (ribonuclease)
6,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the rat prosencephalon it proved possible to differentiate lysosomal ribonuclease from alkaline ribonuclease activity, which could be detected only in the presence of p-chlormercuribenzoate. Acid RNase activity related to the amount of protein in the prosencephalon fell during ontogenesis. It was not significantly affected by four hours' stagnant hypoxia induced by ligation of both carotids. Its release from the lysosomes rose, however (when isotonic homogenates were spun at 20,000 g, acid ribonuclease activity in the supernatants was elevated). The absence of correlation between this activation and the degree of maturity of the nervous tissue refutes the hypothesis that regulation of this enzyme is per se responsible for the known changes induced by hypoxia in the RNA content of the prosencephalon of rats of different ages. On the contrary, the results indirectly support studies which demonstrate changes in the extent of RNA synthesis after hypoxia.
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PMID:Effect of stagnant hypoxia on acid ribonuclease activity in the rat prosencephalon during ontogenesis. 13 32

The action of deoxyribonuclease, ribonuclease, perchloric acid, and pronase on the fine structure of basal bodies of sectioned Paramecium was observed as part of a more extensive autoradiographic electron microscope analysis directed toward the problem of basal body DNA. DNase was found to have no detectable effect on basal body fine structure. Pronase first solubilized the linkers and C tubules of the triplets, then attacked the protein portion of the axosome, a localized portion of the ciliary axoneme adjacent to the distal end of the basal body, the rim fiber, and newly described lumen spiral complex. Prolonged pronase treatment disrupted the remaining microtubular elements, basal body plates, and cartwheel. RNase removed material from the axosome and the lumen complex, a conspicuous structure occupying the central portion of the basal body and consisting of a twisted or looped 90-A diam fiber or, more probably, pair of fibers, in association with large, dense granules. The apparent removal of both RNA and protein from this basal body structure by either of the two corresponding enzymes suggests an unusual organization of the two components. Observations from this and other laboratories suggest that the basal body RNA is single stranded. Its function is unknown but alternatives are discussed.
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PMID:Effects of nuclease and protease digestion on the ultrastructure of Paramecium basal bodies. 17 69

A ribonuclease was isolated and completely purified from sporulating cells of Bacillus subtilis. This RNase has a M.W. of about 150,000 daltons. It hydrolyzes single stranded RNA and single stranded synthetic polynucleotides yielding nucleoside 5'-monophosphates. The enzyme is an exonuclease which degrades polynucleotides from the 3'-end in the direction of the 5'-terminal. The RNase activity is strikingly inhibited by cGMP and to a lesser extent by cAMP. This inhibition (Ki = 0.1 mM) is of a non competitive nature. It appeared that in addition to the inhibition site, the enzyme contains a high affinity binding site for the two cyclic mononucleotides (K (cAMP) = 8.3 x 10-8; K (cGMP) = 2.5 x 10-7). The RNase activity is also strongly inhibited by spermidine. This inhibition appeared to be due to the polyamine binding with the RNA, thus lowering the affinity of the substrate for the active site of the enzyme. This RNase may play a role in vivo in selective degradation of newly synthesized mRNA during sporulation.
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PMID:Isolation and properties of a cyclic guanosine-monophosphate sensitive intracellular ribonuclease from Bacillus subtilis. 18 87

The ribonuclease activity of peripheral lymphocytes from Balb/c mice was studied at various intervals subsequent to infection of mice by oncornavirus. Lymphocytes from mice infected with Friend leukemia virus possessed elevation of RNase activity within 8 days subsequent to infection. Balb/c mice infected with Moloney sarcoma virus demonstrated an analogous elevation of RNase activity with 7-9 days postinfection. Diminishment of cellular RNase activity occurred in the Friend leukemia model concomitant to the occurrence of significant numbers of erythroblasts in the peripheral blood, while ribonuclease activity in lymphocytes from mice infected with Molney sarcoma virus returned to normal 1-2 weeks subsequent to host rejection of tumor. It is concluded that elevation of RNase activity within the lymphocyte represents an early event in oncogenic viral infection within these two tumor models. The possible meaning of elevation of RNase activity is a target (the lymphocyte) not predestined to undergo neoplastic transformation is discussed.
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PMID:Alteration of cellular ribonucleases associated with murine oncogenic virus infection. 20 72

Production of very low density lipoproteins by the liver depends on the cellular availability of fatty acids. It is stimulated by the uptake of free fatty acids from the plasma and by increased lipogenesis and is inhibited by actinomycin D, suggesting that RNA synthesis is involved in the regulation of apolipoprotein synthesis. This hypothesis has been investigated in rats in vivo and in isolated perfused livers with and without stimulation by fatty acid overload: [14C] orotate incorporation in liver polyribosomal RNA is 60 per cent greater in stimulated livers as compared to controls. This increase is primarily due to a higher incorporation in bound polysomes and in those containing at least six ribosomes and does not result from the inhibition of ribonuclease. RNase digestion of polysomal RNA (4.10(-10) M enzyme, 0 degrees C, 3 h) shows that there is twice as much radioactivity in the hydrolyzed RNA of stimulated livers as compared to controls. After partial purification of poly A-rich RNA by affinity chromatography, the mass yield and radioactivity are increased by 100 per cent in stimulated livers as compared to controls. In conclusion, de novo RNA synthesis seems to be necessary for fatty acid stimulation of VLDL production.
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PMID:Ribonucleic acid synthesis in rat liver during fatty acid stimulated secretion of very low density lipoproteins. 21 35

Penicillin stimulates the formation of ribonuclease in embryoless rice (Oryza sativa L.) endosperm and enhances gibberelin-induced response. Penicillin-induced RNase production is completely inhibited by abscisic acid.
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PMID:Penicillin-induced formation of ribonuclease in rice (Oryza sativa L.) endosperm and its inhibition by abscisic acid. 22 13

The ability of RNAase E2 to degradate dinucleoside moniphosphates and to form internucleotide bonds was studied. The compounds of the GpN type were found to be a good substrate for RNase C2. The pH optimum for GpC was 5.5 (acetate buffer) and the temperature optimum was 30 degrees C. The values of Km and Vmax on GpC, GpA, GpG and GpU were determined. The affinity of the substrates for the enzyme decreased in the sequence GpC greater than GpG greater than GpA GREATER THAN GpU. RNase C2 catalyze the synthesis of GpC and GpU. The yield of GpC amounted to 60% and that of GpU was 35%. These data indicate that RNase C2 FROM Asp. clavatum is guanyl ribonuclease (EC 3.1.4.8.).
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PMID:[Specificity of the degradation and synthesis of dinucleoside monophosphates by RNAase C2 of Asp. clavatus]. 23 54

In 8 M urea at low pH, CH3I reacts specifically with the four methionine residues of ribonuclease A, and all four residues react at the same rate. Uon removal of the denaturant, only unmodified ribonuclease and 3 of the 15 possible derivatives modified on methionine refold to regenerate activity. All the enzymatic activity is recored after chromatography on IRC-50 and the four active proteins separate from each other and from the 12 inactive derivatives, which are not eluted from the resin under the conditions used. By the use of 14CH3I, performic acid oxidation, chymotryptic digestion, and separation of the resulting peptides by ion exchange, the active species were determined to be unmodified ribonuclease, CH3Met-29-RNase, CH3Met-79-RNase, and CH3Met-29, CH3Met-79-RNase. these proteins have melting temperatures of 63, 58, 43, and 36 degrees, respectively, at pH 6.3-70. Methylation at methionine-29 or -79 has no effect on enzymatic activity. Conversely, methylation at methionine-13 or -30 prevents refolding to an active conformation at 25 degrees elution from IRC-50. These results are consistent with the positions of the four methionine residues in crystals of ribonuclease A and ribonuclease S as determined by X-ray diffraction.
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PMID:Preparation and properties of three specific active derivatives of ribonuclease A obtained by methylation of methionine residues in 8 M urea. 23 95

From a commercial digestive produced from Aspergillus saitoi, a ribonuclease [EC 3.1.4.23] having a molecular weight of 12,500 has been isolated in addition to the RNase reported previously, which had a molecular weight of 38,000. The enzyme was found to be homogeneous by chromatography on DEAE-cellulose, disc electrophoresis on polyacrylamide gel, and ultracentrifugation. The NH2-terminal amino acid was identified as glutamic acid. The amino acid composition indicated the presence of about 13 tyrosyl residues, 3 histidyl residues, and 2 half-cystine residues. The pH optimum of the RNase was 4.5, using RNA as a substrate. The enzyme was stable on heating at 70 degrees for 5 min from pH 2 to 10. It hydrolysed RNA completely to mononucleotides via 2', 3'-cyclic nucleotides. The rates of release of nucleotides and 2', 3'-cyclic nucleotides were in the order: guanylic acid is greater than adenylic acid is greater than cytidylic acid is greater than uridylic acid.
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PMID:Purification and properties of a new ribonuclease from Aspergillus saitoi. 23 32

The kinetics of the in vitro reconstitution of tobacco mosaic virus from its RNA and protein were studied by measuring the increase in turbidity, the development of ribonuclease-resistant infectivity, the emcapsidation of the terminal ends of the RNA, and the growth of rod length. The results showed that the reconstitution reaction consists of two processes in which the direction, timing, and rate of assembly are different. Rapid elongation of particles toward the 5' end of the RNA proceeds in the first 5-7 min to give intermediate particles of 260 nm in length in which only the 5' terminus of the RNA is encapsidated. The subsequent process requires 30-50 min, is accompanied by a slow increase in turbidity, and gives rise to rods of the full length, 300 nm. The 3' terminus becomes RNase resistant by this process with concomitant development of ribonuclease-resistant infectivity, showing that the 3'-distal portion of the RNA is encapsidated in the direction of 5' to 3'. The rate of rod elongation by the second process is less than 1/10 of that by the first process.
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PMID:Kinetics of biphasic reconstitution of tobacco mosaic virus in vitro. 27 3


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